4E2L

Crystal Structure of the periplasmic domain of mutant FepE LPS O-antigen chain length regulator protein

Summary for 4E2L

• Entry DOI: 10.2210/pdb4e2l/pdb
• Related: 4E29 4E2C 4E2H
• Descriptor: Ferric enterobactin (Enterochelin) transport (1 entity in total)
• Functional Keywords: fepe polysaccharride co-polymerase, wzz, inner membrane, periplasmic space, membrane protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 9
• Total formula weight: 278000.49

Authors

Kalynych, S.,Yao, D.,Magee, J.D.,Cygler, M. (deposition date: 2012-03-08, release date: 2012-03-28, Last modification date: 2024-02-28)

Primary citation

Kalynych, S.,Yao, D.,Magee, J.,Cygler, M.
Structural Characterization of Closely Related O-antigen Lipopolysaccharide (LPS) Chain Length Regulators.
J.Biol.Chem., 287:15696-15705, 2012

PubMed 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.

PubMed: 22437828
DOI: 10.1074/jbc.M112.354837

Experimental method

X-RAY DIFFRACTION (2.8 Å)