Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 24557568Publication DOI: 10.1007/s00253-014-5552-7Journal NLM ID: 8406612Publisher: Springer
Correspondence: pwang11
gsu.edu (P. G. Wang)
Institutions: Center for Diagnostics and Therapeutics and Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA
Bacterial lipopolysaccharide (LPS) is an essential cell envelope component for gram-negative bacteria. As the most variable region of LPS, O antigens serve as important virulence determinants for many bacteria and represent a promising carbohydrate source for glycoconjugate vaccines. In the Wzy-dependent O-antigen biosynthetic pathway, the integral membrane protein Wzy was shown to be the sole enzyme responsible for polymerization of O-repeat unit. Its catalytic mechanism, however, remains elusive. Herein, Wzy was successfully overexpressed in Escherichia coli with an N-terminal His10-tag. Blue native polyacrylamide gel electrophoresis (BN-PAGE) revealed that the Wzy protein exists in its native confirmation as a dimer. Subsequently, we chemo-enzymatically synthesized the substrates of Wzy, the lipid-PP-linked repeat units. Together with an optimized O-antigen visualization method, we monitored the production of reaction intermediates at varying times. We present here our result as the first biochemical evidence that Wzy functions in a distributive manner.
wzy, integral membrane protein, overexpression, distributive mechanism
Structure type: oligomer
Location inside paper: p.4079, fig.3
Aglycon: cis-pentaprenol, monosaturated pentaprenol or undecaprenol
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_143260,IEDB_190606,IEDB_885822,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_88
Methods: SDS-PAGE, ESI-MS, Western blotting, MALDI-TOF MS, genetic methods
Biological activity: biochemical evidence that Wzy polymerizes the repeating unit by a distributive mechanism
Enzymes that release or process the structure: WbnJ
Synthetic data: chemoenzymatic
Related record ID(s): 30164, 30567, 30569, 30570
NCBI Taxonomy refs (TaxIDs): 2162909
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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