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

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DOIResolve DOI: http://doi.org/10.1074/jbc.M112.354837
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TypeArticle
Journal titleThe Journal of Biological Chemistry
ISSN0021-9258
Volume287
Issue19
Pages1569615705; # of pages: 10
AbstractThe 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
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
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This is a non-NRC publication

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NRC number53168
NPARC number21268219
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Record identifier567a1949-1738-4ca4-821e-5119d48c5261
Record created2013-06-05
Record modified2016-05-09
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