4E2C
Crystal Structure of the periplasmic domain of the chimeric LPS O-antigen chain length regulator protein
Summary for 4E2C
| Entry DOI | 10.2210/pdb4e2c/pdb |
| Related | 3B8M 3B8O 3B8P 4E29 4E2H 4E2L |
| Descriptor | chimeric WzzB Chain length determinant protein (2 entities in total) |
| Functional Keywords | chimeric polysaccharide co-polymerase, bacterial inner membrane, membrane protein |
| Biological source | Shigella flexneri More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: Q04866 |
| Total number of polymer chains | 2 |
| Total formula weight | 55476.27 |
| 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 Cited by 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: 22437828DOI: 10.1074/jbc.M112.354837 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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