Yethon JA, Vinogradov E, Perry MB, Whitfield C Mutation of the lipopolysaccharide core glycosyltransferase encoded by waaG destabilizes the outer membrane of Escherichia coli by interfering with phosphorylation Journal of Bacteriology182(19) (2000)
5620-5623
The structure was elucidated in this paper NCBI PubMed ID:10986272 Journal NLM ID:2985120R Publisher: American Society for Microbiology Correspondence: cwhitfieuoguelph.ca Institutions: Canadian Bacterial Diseases Network and Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canadian Bacterial Diseases Network and Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada
In Escherichia coli, phosphoryl substituents in the lipopolysaccharide core region are essential for outer membrane stability. Mutation of the core glucosyltransferase encoded by waaG (formerly rfaG) resulted in lipopolysaccharide truncated immediately after the inner core heptose residues, which serve as the sites for phosphorylation. Surprisingly, mutation of waaG also destabilized the outer membrane. Structural analyses of waaG mutant lipopolysaccharide showed that the cause for this phenotype was a decrease in core phosphorylation, an unexpected side effect of the waaG mutation
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