Language selection

Government of Canada / Gouvernement du Canada

Search

Structural characterization of closely related O-antigen lipopolysaccharide (LPS) chain length regulators

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1074/jbc.M112.354837
AuthorSearch for: ; Search for: ; Search for: ; Search for:
FormatText, Article
Abstract
The surface O-antigen polymers of gram-negative bacteria exhibit a modal length distribution that depends on dedicated chain length regulator periplasmic proteins (polysaccharide co-polymerases, PCPs) anchored in the inner membrane by two transmembrane helices. In an attempt to determine whether structural changes underlie the O-antigen modal length specification, we have determined the crystal structures of several closely related PCPs, namely two chimeric PCP-1 family members solved at 1.6 and 2.8 Å and a wild-type PCP-1 from Shigella flexneri solved at 2.8 Å. The chimeric proteins form circular octamers, whereas the wild-type WzzB from S. flexneri was found to be an open trimer. We also present the structure of a Wzz(FepE) mutant, which exhibits severe attenuation in its ability to produce very long O-antigen polymers. Our findings suggest that the differences in the modal length distribution depend primarily on the surface-exposed amino acids in specific regions rather than on the differences in the oligomeric state of the PCP protomers.
Publication date
PublisherAmerican Society for Biochemistry and Molecular Biology
In
  • The Journal of Biological Chemistry 287, no. 19: 15696–15705.
LanguageEnglish
Peer reviewedYes
NRC publication
This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

NRC numberNRCC 53168
NPARC number21268219
Export citationExport as RIS
Report a correctionReport a correction (opens in a new tab)
Record identifier567a1949-1738-4ca4-821e-5119d48c5261
Record created2013-06-05
Record modified2020-04-21
Date modified: