Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 16839526Publication DOI: 10.1016/j.carres.2006.06.009Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: wang.892
osu.edu
Institutions: Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA, Institute for Biological Sciences, National Research Council of Canada, Ontario, Canada K1A 0R6
The majority of hetero-polysaccharide biosynthesis in Gram-negative bacteria utilizes the wzy-dependent pathway, in which repeating O-units are first synthesized in the cytosol and then subsequently translocated to the periplasmic face of the inner membrane where polymerization is initiated by the Wzy polymerase. Wzy proteins share little primary sequence homology and are specific for their cognate O-unit structures. Our previous studies on O-polysaccharide biosynthesis in Escherichia coli O86 identified the wbnI gene, which encodes a galactosyltransferase responsible for the introduction of α-(1→3)-Galp residues as side chains of the polysaccharide. In this work, we functionally inactivated the wbnI gene and showed that the mutant strain produced a different polysaccharide without the side chain Galp residue. The yield of the polysaccharide was substantially lower than the one produced by the wild-type strain. This study indicated that the complete O-unit structure is the preferred substrate for the polymerization, thus further confirming the specificity of Wzy. On the other hand, these studies also suggest that the Wzy polymerase might have moderate tolerance of side-chain truncated O-unit substrates.
Lipopolysaccharide, glycosyltransferase, polymerization, O-Repeating unit, wzy-Dependent pathway
Structure type: suggested polymer biological repeating unit
Location inside paper: p.2254, fig.1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_140125,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_143260,IEDB_144562,IEDB_149558,IEDB_150766,IEDB_150948,IEDB_150952,IEDB_151528,IEDB_152212,IEDB_152214,IEDB_153207,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461710,IEDB_461718,IEDB_461719,IEDB_885822,IEDB_918314,SB_148,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_86,SB_87,SB_88
Methods: methylation, NMR, MS, composition analysis
Biological activity: serological data
Enzymes that release or process the structure: glycosyltransferase
Biosynthesis and genetic data: genetic data, biosynthetic data
Related record ID(s): 10035, 10195, 10548, 20120, 20328, 20508, 20667, 25273, 108706, 115586
NCBI Taxonomy refs (TaxIDs): 2162909Reference(s) to other database(s): GTC:G75734HT, GlycomeDB:
3571
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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