4E2C

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

4E2C の概要

• エントリーDOI: 10.2210/pdb4e2c/pdb
• 関連するPDBエントリー: 3B8M 3B8O 3B8P 4E29 4E2H 4E2L
• 分子名称: chimeric WzzB Chain length determinant protein (2 entities in total)
• 機能のキーワード: chimeric polysaccharide co-polymerase, bacterial inner membrane, membrane protein
• 由来する生物種: Shigella flexneri; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: Q04866
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55476.27

構造登録者

Kalynych, S.,Yao, D.,Magee, J.D.,Cygler, M. (登録日: 2012-03-08, 公開日: 2012-03-28, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)