Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 16641107Publication DOI: 10.1073/pnas.0509207103Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, CH-8093 Zurich, Switzerland, Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada N1G 2W1, Department of Chemistry and Plant Sciences Institute, Gilman Hall, Iowa State University, Ames, IA 50011-3111, Department of Microbiology and Immunology, University of Western Ontario, London, ON, Canada N6A 5C1
The PglB oligosaccharyltransferase (OTase) of Campylobacter jejuni can be functionally expressed in Escherichia coli, and its relaxed oligosaccharide substrate specificity allows the transfer of different glycans from the lipid carrier undecaprenyl pyrophosphate to an acceptor protein. To investigate the substrate specificity of PglB, we tested the transfer of a set of lipid-linked polysaccharides in E. coli and Salmonella enterica serovar Typhimurium. A hexose linked to the C-6 of the monosaccharide at the reducing end did not inhibit the transfer of the O antigen to the acceptor protein. However, PglB required an acetamido group at the C-2. A model for the mechanism of PglB involving this functional group was proposed. Previous experiments have shown that eukaryotic OTases have the same requirement, suggesting that eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism. Moreover, we demonstrated the functional transfer of the C. jejuni glycosylation system into S. enterica. The elucidation of the mechanism of action and the substrate specificity of PglB represents the foundation for engineering glycoproteins that will have an impact on biotechnology.
LPS, glycoproteins, glycoengineering, PglB, Stt3p
Structure type: oligomer
Location inside paper: p.7090,fig.2
Aglycon: acceptor protein
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_137340,IEDB_140116,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72
Methods: MS
Biological activity: serological data
Comments, role: Glycosylation of AcrA
Related record ID(s): 20109, 20383, 20384, 20386
NCBI Taxonomy refs (TaxIDs): 1010797Reference(s) to other database(s): GTC:G15195YB, GlycomeDB:
27955
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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