Found 3 structures.
Displayed structures from 1 to 3
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1. Compound ID: 10848
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D-gro-a-D-galHepp-(1-2)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-6)-a-D-Manp-(1-3)-a-D-Manp-(1-3)-b-D-S6Fucp-(1-4)-b-D-Glcp-(1-3)-b-D-Galp1N-(1-4)-Asn |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_141793,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_983930,IEDB_983931,SB_192,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73
The structure is contained in the following publication(s):
- Article ID: 4412
Vinogradov E, Deschatelets L, Lamoureux M, Patel GB, Tremblay TL, Robotham A, Goneau MF, Cummings-Lorbetskie C, Watson DC, Brisson JR, Kelly JF, Gilbert M "Cell surface glycoproteins from Thermoplasma acidophilum are modified with an N-linked glycan containing 6-C-sulfofucose" -
Glycobiology 22(9) (2012) 1256-1267
Thermoplasma acidophilum is a thermoacidophilic archaeon that grows optimally at pH 2 and 59 degrees C. This extremophile is remarkable by the absence of a cell wall or an S-layer. Treating the cells with Triton X-100 at pH 3 allowed the extraction of all of the cell surface glycoproteins while keeping cells intact. The extracted glycoproteins were partially purified by cation-exchange chromatography, and we identified five glycoproteins by N-terminal sequencing and mass spectrometry of in-gel tryptic digests. These glycoproteins are positive for periodic acid-Schiff staining, have a high content of Asn including a large number in the Asn-X-Ser/Thr sequon and have apparent masses that are 34-48% larger than the masses deduced from their amino acid sequences. The pooled glycoproteins were digested with proteinase K and the purified glycopeptides were analyzed by NMR. Structural determination showed that the carbohydrate part was represented by two structures in nearly equal amounts, differing by the presence of one terminal mannose residue. The larger glycan chain consists of eight residues: six hexoses, one heptose and one sugar with an unusual residue mass of 226 Da which was identified as 6-deoxy-6-C-sulfo-D-galactose (6-C-sulfo-D-fucose). Mass spectrometry analyses of the peptides obtained by trypsin and chymotrypsin digestion confirmed the principal structures to be those determined by NMR and identified 14 glycopeptides derived from the main glycoprotein, Ta0280, all containing the Asn-X-Ser/Thr sequons. Thermoplasma acidophilum appears to have a 'general' protein N-glycosylation system that targets a number of cell surface proteins.
glycoprotein, Thermoplasma, N-linked glycan, sulfofucose
NCBI PubMed ID: 22692048Publication DOI: 10.1093/glycob/cws094Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: michel.gilbert@nrc-cnrc.gc.ca
Institutions: Human Health Therapeutics, National Research Council Canada, Ottawa, Ontario, Canada K1A 0R6
Methods: 13C NMR, 1H NMR, SDS-PAGE, chemical analysis, conformation analysis, MS/MS, enzymatic digestion, molecular modeling, LC-MS
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2. Compound ID: 10849
|
D-gro-a-D-galHepp-(1-2)-+
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a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-3)-a-D-Manp-(1-3)-b-D-S6Fucp-(1-4)-b-D-Glcp-(1-3)-b-D-Galp1N-(1-4)-Asn |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_141793,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_983930,IEDB_983931,SB_192,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73
The structure is contained in the following publication(s):
- Article ID: 4412
Vinogradov E, Deschatelets L, Lamoureux M, Patel GB, Tremblay TL, Robotham A, Goneau MF, Cummings-Lorbetskie C, Watson DC, Brisson JR, Kelly JF, Gilbert M "Cell surface glycoproteins from Thermoplasma acidophilum are modified with an N-linked glycan containing 6-C-sulfofucose" -
Glycobiology 22(9) (2012) 1256-1267
Thermoplasma acidophilum is a thermoacidophilic archaeon that grows optimally at pH 2 and 59 degrees C. This extremophile is remarkable by the absence of a cell wall or an S-layer. Treating the cells with Triton X-100 at pH 3 allowed the extraction of all of the cell surface glycoproteins while keeping cells intact. The extracted glycoproteins were partially purified by cation-exchange chromatography, and we identified five glycoproteins by N-terminal sequencing and mass spectrometry of in-gel tryptic digests. These glycoproteins are positive for periodic acid-Schiff staining, have a high content of Asn including a large number in the Asn-X-Ser/Thr sequon and have apparent masses that are 34-48% larger than the masses deduced from their amino acid sequences. The pooled glycoproteins were digested with proteinase K and the purified glycopeptides were analyzed by NMR. Structural determination showed that the carbohydrate part was represented by two structures in nearly equal amounts, differing by the presence of one terminal mannose residue. The larger glycan chain consists of eight residues: six hexoses, one heptose and one sugar with an unusual residue mass of 226 Da which was identified as 6-deoxy-6-C-sulfo-D-galactose (6-C-sulfo-D-fucose). Mass spectrometry analyses of the peptides obtained by trypsin and chymotrypsin digestion confirmed the principal structures to be those determined by NMR and identified 14 glycopeptides derived from the main glycoprotein, Ta0280, all containing the Asn-X-Ser/Thr sequons. Thermoplasma acidophilum appears to have a 'general' protein N-glycosylation system that targets a number of cell surface proteins.
glycoprotein, Thermoplasma, N-linked glycan, sulfofucose
NCBI PubMed ID: 22692048Publication DOI: 10.1093/glycob/cws094Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: michel.gilbert@nrc-cnrc.gc.ca
Institutions: Human Health Therapeutics, National Research Council Canada, Ottawa, Ontario, Canada K1A 0R6
Methods: 13C NMR, 1H NMR, SDS-PAGE, chemical analysis, conformation analysis, MS/MS, enzymatic digestion, molecular modeling, LC-MS
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3. Compound ID: 16587
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D-gro-a-D-galHepp-(1-2)-+
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a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-6)-a-D-Manp-(1-3)-a-D-Manp-(1-3)-b-D-S6Fucp-(1-4)-b-D-Glcp-(1-3)-b-D-Galp1N-(1-4)-Asn-(?--/Asn-peptide/ |
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Structure type: oligomer
Aglycon: Asn-peptide
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_141793,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_983930,IEDB_983931,SB_192,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73
The structure is contained in the following publication(s):
- Article ID: 6434
Notaro A, Zaretsky M, Molinaro A, De Castro C, Eichler J "N-glycosylation in Archaea: Unusual sugars and unique modifications" -
Carbohydrate Research 534 (2023) 108963
Archaea are microorganisms that comprise a distinct branch of the universal tree of life and which are best known as extremophiles, residing in a variety of environments characterized by harsh physical conditions. One seemingly universal trait of Archaea is the ability to perform N-glycosylation. At the same time, archaeal N-linked glycans present variety in terms of both composition and architecture not seen in the parallel eukaryal or bacterial processes. In this mini-review, many of the unique and unusual sugars found in archaeal N-linked glycans as identified by nuclear magnetic resonance spectroscopy are described.
nuclear magnetic resonance spectroscopy, glycan structure, archaea, N-glycosylation, Extremophiles
NCBI PubMed ID: 37890267Publication DOI: 10.1016/j.carres.2023.108963Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: J. Eichler
Institutions: Department of Agricultural Sciences, University of Napoli Federico II, Portici, Italy, Department of Life Sciences, Ben-Gurion University of the Negev, Beersheva, Israel, Department of Chemical Sciences, University of Napoli Federico II, Napoli, Italy
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