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Heinrichs DE, Monteiro MA, Perry MB, Whitfield C
The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica. Structure and function of the r2 waak and waal homologs
Journal of Biological Chemistry 273(15) (1998)
8849-8859
|
a-D-Galp-(1-6)-+
|
a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp-(1-3)-D-gro-a-D-manHepp-(1--/Kdo-lipid A/ |
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Escherichia coli R2
(Ancestor NCBI TaxID 562,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 9535865Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: cwhitfie
uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A OR6
In Escherichia coli F632, the 14-kilobase pair chromosomal region located between waaC (formerly rfaC) and waaA (kdtA) contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90% total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and waaL (rfaL) each resemble homologs in Salmonella enterica serovar Typhimurium but share little similarity with E. coli K-12. The F632 WaaK and WaaL proteins therefore define differences between the type R2 and K-12 outer core oligosaccharides of E. coli lipopolysaccharides. Based on the chemical structure of the core oligosaccharide of an E. coli F632 waaK::aacC1 mutant and in vitro glycosyltransferase analyses, waaK encodes UDP-N-acetylglucosamine:(glucose) lipopolysaccharide a1,2-N-acetylglucosaminyltransferase. The WaaK enzyme adds a terminal GlcNAc side branch substituent that is crucial for the recognition of core oligosaccharide acceptor by the O-polysaccharide ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that structural differences between the WaaL proteins play a role in recognition of, and interaction with, terminal lipopolysaccharide core moieties.
Lipopolysaccharide, biosynthesis, structure, core, Escherichia, Escherichia coli, Salmonella, assembly, homolog, Salmonella enterica, function, hybrid
Structure type: oligomer
Location inside paper: Fig. 1
Aglycon: Kdo-lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_232584,IEDB_983931,SB_192,SB_7
Methods: methylation, PCR, DNA sequencing, FAB-MS, NMR, SDS-PAGE, enzymatic digestion, DNA restriction, endonuclease ligation
Enzymes that release or process the structure: endonuclease
Biosynthesis and genetic data: biosynthetic data, genetic data
Comments, role: outer core
Related record ID(s): 2554, 2555
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G83625PL, GlycomeDB:
25635
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There is only one chemically distinct structure:
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Heinrichs DE, Monteiro MA, Perry MB, Whitfield C
The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica. Structure and function of the r2 waak and waal homologs
Journal of Biological Chemistry 273(15) (1998)
8849-8859
|
a-D-Galp-(1-6)-+
|
D-gro-a-D-manHepp-(1-6)-a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp-(1-3)-D-gro-a-D-manHepp-(1--/Kdo-Lipid A/ |
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Escherichia coli K12
(NCBI TaxID 83333,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 ]
NCBI PubMed ID: 9535865Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: cwhitfie
uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A OR6
In Escherichia coli F632, the 14-kilobase pair chromosomal region located between waaC (formerly rfaC) and waaA (kdtA) contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90% total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and waaL (rfaL) each resemble homologs in Salmonella enterica serovar Typhimurium but share little similarity with E. coli K-12. The F632 WaaK and WaaL proteins therefore define differences between the type R2 and K-12 outer core oligosaccharides of E. coli lipopolysaccharides. Based on the chemical structure of the core oligosaccharide of an E. coli F632 waaK::aacC1 mutant and in vitro glycosyltransferase analyses, waaK encodes UDP-N-acetylglucosamine:(glucose) lipopolysaccharide a1,2-N-acetylglucosaminyltransferase. The WaaK enzyme adds a terminal GlcNAc side branch substituent that is crucial for the recognition of core oligosaccharide acceptor by the O-polysaccharide ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that structural differences between the WaaL proteins play a role in recognition of, and interaction with, terminal lipopolysaccharide core moieties.
Lipopolysaccharide, biosynthesis, structure, core, Escherichia, Escherichia coli, Salmonella, assembly, homolog, Salmonella enterica, function, hybrid
Structure type: oligomer
Location inside paper: Fig. 1
Aglycon: Kdo-Lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_190606,IEDB_2189046,IEDB_232584,IEDB_983931,SB_192,SB_7
Methods: methylation, PCR, DNA sequencing, FAB-MS, NMR, SDS-PAGE, enzymatic digestion, DNA restriction, endonuclease ligation
Enzymes that release or process the structure: endonuclease
Biosynthesis and genetic data: biosynthetic data, genetic data
Comments, role: outer core
Related record ID(s): 2408, 2555
NCBI Taxonomy refs (TaxIDs): 83333Reference(s) to other database(s): GTC:G07524IO, GlycomeDB:
25708
Show glycosyltransferases
There is only one chemically distinct structure:
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Heinrichs DE, Monteiro MA, Perry MB, Whitfield C
The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica. Structure and function of the r2 waak and waal homologs
Journal of Biological Chemistry 273(15) (1998)
8849-8859
|
a-D-Galp-(1-6)-+
|
a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1-3)-D-gro-a-D-manHepp-(1--/Kdo-Lipid A/ |
Show graphically |
Salmonella enterica
(NCBI TaxID 28901,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Salmonella enterica [ICD11:
XN5VC ]
NCBI PubMed ID: 9535865Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: cwhitfie
uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A OR6
In Escherichia coli F632, the 14-kilobase pair chromosomal region located between waaC (formerly rfaC) and waaA (kdtA) contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90% total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and waaL (rfaL) each resemble homologs in Salmonella enterica serovar Typhimurium but share little similarity with E. coli K-12. The F632 WaaK and WaaL proteins therefore define differences between the type R2 and K-12 outer core oligosaccharides of E. coli lipopolysaccharides. Based on the chemical structure of the core oligosaccharide of an E. coli F632 waaK::aacC1 mutant and in vitro glycosyltransferase analyses, waaK encodes UDP-N-acetylglucosamine:(glucose) lipopolysaccharide a1,2-N-acetylglucosaminyltransferase. The WaaK enzyme adds a terminal GlcNAc side branch substituent that is crucial for the recognition of core oligosaccharide acceptor by the O-polysaccharide ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that structural differences between the WaaL proteins play a role in recognition of, and interaction with, terminal lipopolysaccharide core moieties.
Lipopolysaccharide, biosynthesis, structure, core, Escherichia, Escherichia coli, Salmonella, assembly, homolog, Salmonella enterica, function, hybrid
Structure type: oligomer
Location inside paper: Fig. 1
Aglycon: Kdo-Lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_983931,SB_192,SB_7
Methods: methylation, PCR, DNA sequencing, FAB-MS, NMR, SDS-PAGE, enzymatic digestion, DNA restriction, endonuclease ligation
Enzymes that release or process the structure: endonuclease
Biosynthesis and genetic data: biosynthetic data, genetic data
Comments, role: outer core
Related record ID(s): 2408, 2554
NCBI Taxonomy refs (TaxIDs): 28901Reference(s) to other database(s): GTC:G75408UN, GlycomeDB:
25648
Show glycosyltransferases
There is only one chemically distinct structure:
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