Found 24 structures.
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1. Compound ID: 1470
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GroA-(2--P--4)--b-D-ManpNAc-(1-4)-+
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a-D-Glcp-(1-6)-+ |
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{{{-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-}}}/n=21/-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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2. Compound ID: 1471
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Me-3)-{{{-a-L-Rhap-(1-4)-a-D-Manp-(1-3)-}}}/n=28/-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_137477,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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3. Compound ID: 1472
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b-D-Galf-(1-3)-a-D-Galp-(1-2)-a-L-Rhap-(1-3)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-b-D-Glcp-(1-?)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_189517,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_7,SB_72
The structure is contained in the following publication(s):
- Article ID: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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4. Compound ID: 1474
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b-D-Glcp-(1-6)-+
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b-D-Glcp-(1-6)-+ |
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a-D-Galp-(1-2)-+ | a-D-Galp-(1-2)-+ |
| | | |
{{{-a-L-Rhap-(1-3)-a-D-Manp-(1-4)-b-L-Rhap-(1-3)-a-D-Glcp-(1-4)-}}}/n=4-11/-a-L-Rhap-(1-3)-a-D-Manp-(1-4)-b-L-Rhap-(1-3)-b-D-Glcp-(1-7)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_7,SB_72
The structure is contained in the following publication(s):
- Article ID: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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5. Compound ID: 3456
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a-D-Manp-(1-4)-+
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b-D-Glcp-(1-4)-b-D-S6Quip-(1-3)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-1)-Tyr-(2-1)-Asn
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a-D-Manp-(1-6)-+ |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_141807,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_72,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 1312
Zähringer U, Moll H, Hettmann T, Knirel YA, Schafer G "Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose" -
European Journal of Biochemistry 267(13) (2000) 4144-4149
Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius (DSM 639) has been described as a novel highly glycosylated membrane-bound b-type hemoprotein [Hettmann, T., Schmidt, C. L., Anemuller, S., Zähringer, U., Moll, Haemophilus, Petersen, A. & Schafer, G. (1998) J. Biol. Chem. 273, 12032-12040]. The purified cytochrome b558/566 was characterized by MALDI MS as a 64-kDa (glyco)protein expressing 17% glycosylation. Detailed chemical studies showed that it was exclusively O-mannosylated with monosaccharides and N-glycosylated with at least seven hexasaccharide units having the same unique structure. The hexasaccharide was released by cleavage with peptide:N-glycosidase (PNGase) F and found to consist of two residues each of Man and GlcNAc and one residue each of Glc and 6-deoxy-6-sulfoglucose (6-sulfoquinovose). The last sugar has been known as a component of glycolipids of plants and some prokaryotes, but has not been hitherto found in bacterial glycoproteins. Digestion with trypsin/pronase gave a mixture of glycopeptides with the same Asn-linked hexasaccharide chain, from which an N-glycosylated Tyr-Asn dipeptide was purified by gel chromatography and anion-exchange HPLC. Studies of the degradation products using methylation analysis, ESI MS, MALDI MS, and 1H and 13C NMR spectroscopy, including 1H,13C HMQC and NOESY experiments, established the structure of the unique Asn-linked hexasaccharide chain of cytochrome b558/566
structure, branched, hexasaccharide, chain, glycopeptide, glycoprotein, Archaeon, 6-sulfoquinovose
NCBI PubMed ID: 10866817Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: uzaehr@fz-borstel.de
Institutions: Forschungszentrum Borstel, Zentrum fur Medizin und Biowissenschaften, Borstel, Germany
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6. Compound ID: 5645
Structure type: oligomer
Compound class: O-glycoprotein
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 2451
Lis H, Sharon N "Protein glycosylation. Structural and functional aspects" -
European Journal of Biochemistry 218 (1993) 1-27
During the last decade, there have been enormous advances in our knowledge of glycoproteins and the stage has been set for the biotechnological production of many of them for therapeutic use. These advances are reviewed, with special emphasis on the structure and function of the glycoproteins (excluding the proteoglycans). Current methods for structural analysis of glycoproteins are surveyed, as are novel carbohydrate-peptide linking groups, and mono- and oligo-saccharide constituents found in these macromolecules. The possible roles of the carbohydrate units in modulating the physicochemical and biological properties of the parent proteins are discussed, and evidence is presented on their roles as recognition determinants between molecules and cells, or cell and cells. Finally, examples are given of changes that occur in the carbohydrates of soluble and cell-surface glycoproteins during differentiation, growth and malignancy, which further highlight the important role of these substances in health and disease.
NCBI PubMed ID: 8243456Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel
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7. Compound ID: 5872
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b-D-Galf-(1-3)-a-D-Galp-(1-2)-a-L-Rhap-(1-3)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-b-D-Glcp-(1-7)-Tyr |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_189517,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_7,SB_72
The structure is contained in the following publication(s):
- Article ID: 2596
Messner P, Christian R, Kolbe J, Schulz G, Sleytr UB "Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70" -
Journal of Bacteriology 174 (1992) 2236-2240
Journal NLM ID: 2985120RPublisher: American Society for Microbiology
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8. Compound ID: 6121
Structure type: oligomer
Compound class: O-glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 2730
Herrmann GF, Wang P, Shen GJ, Garcia-Junceda E, Khan SH, Matta KL, Wong CH "Large scale production of recombinant a-1,2-mannosyltransferase from E. coli for the study of acceptor specificity and use of the recombinant whole cells in synthesis" -
Journal of Organic Chemistry 59 (1994) 6356-6362
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9. Compound ID: 6379
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GroA-(2--P--4)--b-D-ManpNAc-(1-4)-+
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a-D-Glcp-(1-6)-+ a-D-Glcp-(1-6)-+ a-D-Glcp-(1-6)-+ |
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b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-{{{-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-}}}/n=20/-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-1)-Tyr |
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Structure type: oligomer
Trivial name: O-linked glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 2877
Messner P, Christian R, Neuninger C, Schulz G "Similarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins" -
Journal of Bacteriology 177 (1995) 2188-2193
Previously, the repeating-unit structure of the S-layer glycoprotein from the eubacterium Bacillus alvei CCM 2051 has been determined to be [→3)-β-D-Galp-(1→4)-[α-D-Glcp-(1→6)-]-β-D-ManpNAc-(1→]n (E. Altman, J.-R. Brisson, P. Messner, and U. B. Sleytr, Biochem. Cell Biol. 69:72-78, 1991). Nuclear magnetic resonance spectroscopic reexamination of this glycan reveals that the O-antigen-like domain of the polysaccharide is [see text] connected with the S-layer polypeptide through the "core" structure →3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-β-D-Galp-(1→O)-Tyr. Except for the substitution in position 4 of the nonreducing rhamnose with the modified glyceric acid phosphate residue GroA-2→OPO2→4-β-D-ManpNAc-(1→, this core is identical to the core of the tyrosine-linked glycan from the S-layer glycoprotein of Thermoanaerobacter thermohydrosulfuricus L111-69 (K. Bock, J. Schuster-Kolbe, E. Altman, G. Allmaier, B. Stahl, R. Christian, U. B. Sleytr, and P. Messner, J. Biol. Chem. 269:7137-7144, 1994).
NCBI PubMed ID: 7721708Publication DOI: 10.1128/jb.177.8.2188-2193.1995Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Institutions: Zentrum für Ultrastrukturforschung, Universität für Bodenkultur, Vienna, Austria
Methods: 13C NMR, 1H NMR
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10. Compound ID: 7306
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Subst-(1-4)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr
Subst = glycan chain (ID 22503) |
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Structure type: oligomer
Trivial name: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 3310
Bock K, Schuster-Kolbe J, Altman E, Allmaier G, Stahl B, Christian R, Sleytr UB, Messner P "Primary structure of the O-glycosidically linked glycan chain of the crystalline surface layer glycoprotein of Thermoanaerobacter thermohydrosulfuricus L111-69. Galactosyl tyrosine as a novel linkage unit" -
Journal of Biological Chemistry 269(10) (1994) 7137-7144
The products of Pronase digestion of the crystalline surface layer (S-layer) glycoproteins of Thermoanaerobacter thermohydrosulfuricus strains L111-69 and L110-69 were isolated by gel permeation chromatography, cation exchange chromatography, chromatofocusing, and reversed phase high performance liquid chromatography. Four compounds were obtained which were analyzed by monosaccharide analysis, one- and two-dimensional 500 and 600 MHz 1H and 13C NMR spectroscopy, methylation analysis, gas-liquid chromatography/mass spectrometry, and matrix-assisted laser desorption ionization mass spectrometry. For all glycopeptides we propose the following glycan structure with galactose as the linkage sugar. [formula: see text] The isolated glycopeptides resulted from Pronase cleavage at the glycosylated tyrosine residues. Tyrosine was found as the linkage amino acid in all fractions but the remaining amino acid sequences varied, indicating the presence of different glycosylation sites in the intact S-layer glycoprotein
NMR spectroscopy, amino acid, S-layer, Clostridium, glycoprotein, Pronase
NCBI PubMed ID: 8125923Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Chemistry, Carlsberg Laboratory, Valby, Copenhagen, Denmark
Methods: 13C NMR, 1H NMR, methylation, NMR-2D, mild acid hydrolysis, MALDI-MS, alkaline hydrolysis, analytical methods, enzymatic digestion
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11. Compound ID: 8271
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b-D-Galf-(1-3)-a-D-Galp-(1-2)-a-L-Rhap-(1-3)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-b-D-Glcp-(1-7)-L-Tyr |
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Structure type: oligomer
; 87500-94000
Trivial name: S-layer glycan
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_189517,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_7,SB_72
The structure is contained in the following publication(s):
- Article ID: 3619
Christian R, Schulz G, Schuster-Kolbe J, Allmaier G, Schmid ER, Sleytr UB, Messner P "Complete structure of the tyrosine-linked saccharide moiety from the surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70" -
Journal of Bacteriology 175(5) (1993) 1250-1256
In this study, we have extended and completed a previous investigation (P. Messner, R. Christian, J. Kolbe, G. Schulz, and U. B. Sleytr, J. Bacteriol. 174:2236-2240, 1992) in which we demonstrated for the first time in prokaryotic organisms the presence of a novel O-glycosidic linkage via tyrosine. The surface layer glycoprotein of the eubacterium Clostridium thermohydrosulfuricum S102-70 is arranged in a hexagonal lattice, with center-to-center spacings of approximately 16.3 nm. Molecular weight determination by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of both glycosylated and chemically deglycosylated surface layer glycoprotein showed values for the monomeric subunits of 94,000 and 87,500, respectively. Glycopeptide fractions obtained after exhaustive pronase digestion of purified, intact glycoprotein were isolated by reversed-phase liquid chromatography. One- and two-dimensional nuclear magnetic resonance studies, together with chemical analyses and plasma desorption time-of-flight mass spectrometry, were used to elucidate the structure of the hexasaccharide moiety linked by the novel O-glycosidic linkage to tyrosine. The combined evidence suggests the following structure: β-D-Galf-(1→3)-α-D-Galp- (1→2)-α-L-Rhap-(1→3)-α-D-Manp-(1→3)-α-L-Rhap-(1→3)-β- D-Glcp-(1→4)-L-Tyr.
structure, mass spectrometry, Clostridium, glycoprotein, tyrosine
NCBI PubMed ID: 8444787Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Institutions: Zentrum für Ultrastrukturforschung, Universität für Bodenkultur, Vienna, Austria
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, chemical analysis, PD-MS, NMR-1D, electron microscopy, deglycosylation
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12. Compound ID: 9308
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GroA-(2--P--4)--b-D-ManpNAc-(1-4)-+
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a-D-Glcp-(1-6)-+ |
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{{{-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-}}}/n=24/-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr-(?--/tyrosine residues of the S-layer protein backbone/ |
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Structure type: oligomer
Aglycon: tyrosine residues of the S-layer protein backbone
Trivial name: S-layer O-glycan
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 3967
Zarschler K, Janesch B, Pabst M, Altmann F, Messner P, Schäffer C "Protein tyrosine O-glycosylation - A rather unexplored prokaryotic glycosylation system" -
Glycobiology 20(6) (2010) 787-798
lycosylation is a frequent and heterogeneous posttranslational protein modification occurring in all domains of life. While protein N-glycosylation at asparagine and O-glycosylation at serine, threonine or hydroxyproline residues have been studied in great detail, only few data are available on O-glycosidic attachment of glycans to the amino acid tyrosine. In this study, we describe the identification and characterization of a bacterial protein tyrosine O-glycosylation system. In the Gram-positive, mesophilic bacterium Paenibacillus alvei CCM 2051T, a polysaccharide consisting of [→3)-β-D-Galp-(1[α-D-Glcp-(1→6)] →4)-β-D-ManpNAc-(1→] repeating units is O-glycosidically linked via an adaptor with the structure -[GroA-2→OPO2→4-β-D-ManpNAc-(1→4)] →3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-β-D-Galp-(1→ to specific tyrosine residues of the S-layer protein SpaA. A +AH4-24.3-kb S-layer glycosylation (slg) gene cluster encodes the information necessary for the biosynthesis of this glycan chain within 18 open reading frames (ORF). The corresponding translation products are involved in the biosynthesis of nucleotide-activated monosaccharides, assembly and export as well as in the transfer of the completed polysaccharide chain to the S-layer target protein. All ORFs of the cluster, except those encoding the nucleotide sugar biosynthesis enzymes and the ATP binding cassette (ABC) transporter integral transmembrane proteins, were disrupted by the insertion of the mobile group II intron Ll.LtrB, and S-layer glycoproteins produced in mutant backgrounds were analyzed by mass spectrometry. There is evidence that the glycan chain is synthesized in a process comparable to the ABC-transporter-dependent pathway of the lipopolysaccharide O-polysaccharide biosynthesis. Furthermore, with the protein WsfB, we have identified an O-oligosaccharyl:protein transferase required for the formation of the covalent β-D-Gal→Tyr linkage between the glycan chain and the S-layer protein.
S-layer, glycosylation gene cluster, Paenibacillus alvei, tyrosine O-glycosylation
NCBI PubMed ID: 20200052Publication DOI: 10.1093/glycob/cwq035Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boku.ac.at; christina.schae?er@boku.ac.at
Institutions: Department of NanoBiotechnology, Vienna Institute of BioTechnology, Universitat fur Bodenkultur Wien, A-1190 Vienna, Austria
Methods: PCR, SDS-PAGE, DNA techniques, ESI-MS, genetic methods, RT-PCR, LC-MS
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13. Compound ID: 14054
|
L-Tyr-(1-5)-b-D-Allf1N5NA-(1-1)-Subst
All1N5NA = 1,5-diamino-1,5-deoxy-alluronic acid;
Subst = 4-formyl-4-imidazolin-2-one = SMILES O=Cc1c{1}[nH]c(=O)[nH]1 |
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Structure type: monomer
; 449 [M-H]-
Trivial name: nikkomycin Wx
Compound class: glycoside
The structure is contained in the following publication(s):
- Article ID: 5550
Decker H, Walz F, Bormann C, Zähner H, Fiedler HP, Heitsch H, Konig WA "Metabolic products of microorganisms. 255. Nikkomycins Wz and Wx, new chitin synthetase inhibitors from Streptomyces tendae" -
The Journal of Antibiotics 43(1) (1990) 43-48
Two new dipeptidyl nikkomycins of the Z and X type were isolated from the culture broth of Streptomyces tendae TÜ 901/395-11/32 and characterized. They show a variation in the amino acid moiety of the molecule. Nikkomycin Wz is composed of L-tyrosine and 5-amino-5-deoxy-D-allo-furanuronic acid N-glycosidally bound to uracil, whereas nikkomycin Wx is composed of L-tyrosine and 5-amino-5-deoxy-D-allo-furanuronic acid N-glycosidally bound to 4-formyl-4-imidazolin-2-one. The new nikkomycins are good inhibitors of chitin synthetase from Coprinus cinereus but they did not inhibit growth of fungi and yeasts
antibiotics, nikkomycins, Streptomyces tendae
NCBI PubMed ID: 2137814Publication DOI: 10.7164/antibiotics.43.43Journal NLM ID: 0151115Publisher: London: Nature Publishing Group
Institutions: Biologisches Institut, LB Mikrobiologie/Antibiotika, Universität Tübingen, Tübingen, Germany, Institut für Organische Chemie, Universität Hamburg, Hamburg, Germany
Methods: 1H NMR, methylation, FAB-MS, GC-MS, acid hydrolysis, biological assays, HPLC, extraction, acetylation, CC, cell growth, mutagenesis, enzymatic assay
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14. Compound ID: 14055
|
L-Tyr-(1-5)-b-D-Allf1N5NA-(1-1)-Subst
All1N5NA = 1,5-diamino-1,5-deoxy-alluronic acid;
Subst = uracil = SMILES O=c1cc{1}[nH]c(=O)[nH]1 |
Show graphically |
Structure type: monomer
; 449 [M-H]-
Trivial name: nikkomycin Wz
Compound class: glycoside
The structure is contained in the following publication(s):
- Article ID: 5550
Decker H, Walz F, Bormann C, Zähner H, Fiedler HP, Heitsch H, Konig WA "Metabolic products of microorganisms. 255. Nikkomycins Wz and Wx, new chitin synthetase inhibitors from Streptomyces tendae" -
The Journal of Antibiotics 43(1) (1990) 43-48
Two new dipeptidyl nikkomycins of the Z and X type were isolated from the culture broth of Streptomyces tendae TÜ 901/395-11/32 and characterized. They show a variation in the amino acid moiety of the molecule. Nikkomycin Wz is composed of L-tyrosine and 5-amino-5-deoxy-D-allo-furanuronic acid N-glycosidally bound to uracil, whereas nikkomycin Wx is composed of L-tyrosine and 5-amino-5-deoxy-D-allo-furanuronic acid N-glycosidally bound to 4-formyl-4-imidazolin-2-one. The new nikkomycins are good inhibitors of chitin synthetase from Coprinus cinereus but they did not inhibit growth of fungi and yeasts
antibiotics, nikkomycins, Streptomyces tendae
NCBI PubMed ID: 2137814Publication DOI: 10.7164/antibiotics.43.43Journal NLM ID: 0151115Publisher: London: Nature Publishing Group
Institutions: Biologisches Institut, LB Mikrobiologie/Antibiotika, Universität Tübingen, Tübingen, Germany, Institut für Organische Chemie, Universität Hamburg, Hamburg, Germany
Methods: 1H NMR, methylation, FAB-MS, GC-MS, acid hydrolysis, biological assays, HPLC, extraction, acetylation, CC, cell growth, mutagenesis, enzymatic assay
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15. Compound ID: 14143
| Cyclic
Subst2-(1-2)-D-aThr-(1-2)-+ b-D-Manp-(1-3)-+
| |
-3)-Thr-(1-2)-Thr-(1-2)-D-Tyr-(1-2)-Subst-(1-2)-Gln-(1-2)-Gly-(1-2)-Thr2Me-(1-2)-Gln-(1-
Subst = (2Z)-2-aminobut-2-enoic acid = SMILES C/C={2}C(N)\{1}C(=O)O;
Subst2 = 2,3-dihydroxymyristic acid = SMILES CCCCCCCCCCCC(O)C(O){1}C(=O)O |
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Structure type: cyclic polymer repeating unit
; 1404.67572 [M+Na]+, n=1
C62H99N11O24
Trivial name: hassalidin A
Compound class: glycopeptide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72
The structure is contained in the following publication(s):
- Article ID: 5580
Neuhof T, Schmieder P, Preussel K, Dieckmann R, Pham H, Bartl F, von Döhren H "Hassallidin A, a glycosylated lipopeptide with antifungal activity from the cyanobacterium Hassallia sp." -
Journal of Natural Products 68(5) (2005) 695-700
Hassallidin A (1), a new antifungal glycosylated lipopeptide, was isolated from an epilithic cyanobacterium collected in Bellano, Italy, identified as Tolypothrix (basionym Hassallia) species. Chemical, mass spectrometric, and spectroscopic analyses, including one- and two-dimensional NMR, were performed to determine an esterified eight-residue cyclic peptide linked with a carbohydrate and a fatty acid residue. Chiral GC-MS analysis revealed the occurrence of the nonproteinogenic amino acids D-allo-Thr, D-Thr, D-Tyr, D-Gln, and dehydroaminobutyric acid (Dhb) within the peptide moiety. The additional components of hassallidin A could be identified as alpha,beta-dihydroxytetradecanoic acid (Dht) and mannose. This is the first report on a cyclic peptide of cyanobacterial origin that contains both a fatty acid and a carbohydrate moiety. Compound 1 exhibits antifungal activity against Aspergillus fumigatus and Candida albicans with MIC values of 4.8 μg/mL for both test organisms
hassalidin A, antifungal activity, Tolypothrix, cyclic peptide
NCBI PubMed ID: 15921412Publication DOI: 10.1021/np049671rJournal NLM ID: 7906882Publisher: American Society of Pharmacognosy
Correspondence: doehren@chem.tu-berlin.de
Institutions: Institut für Chemie, Fak. II, Technische Universität Berlin, Berlin, Germany, Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany, Institut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Humboldt-Universität, Berlin, Germany, Zentrum für Biophysik und Bioinformatik, Humboldt-Universität, Berlin, Germany
Methods: 13C NMR, 1H NMR, NMR-2D, IR, GC-MS, ESI-MS, acid hydrolysis, ESI-ICR-MS, amino acid analysis, MALDI-TOF MS, HPLC, UV, extraction, 15N NMR, cell growth, derivatization, evaporation, centrifugation, antifungal activity test, optical density measurement
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