2V04

CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE

2V04 の概要

• エントリーDOI: 10.2210/pdb2v04/pdb
• 関連するPDBエントリー: 2V05
• 分子名称: CHOLINE BINDING PROTEIN F, CHOLINE ION (3 entities in total)
• 機能のキーワード: cbpf, choline-binding-protein, lipid-binding-protein, lipid binding protein
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37052.14

構造登録者

Hermoso, J.,Molina, R.,Kahn, R.,Stelter, M. (登録日: 2007-05-08, 公開日: 2008-06-10, 最終更新日: 2024-05-08)

主引用文献

Molina, R.,Gonzalez, A.,Stelter, M.,Perez-Dorado, I.,Kahn, R.,Morales, M.,Campuzano, S.,Campillo, N.E.,Mobashery, S.,Garcia, J.L.,Garcia, P.,Hermoso, J.A.
Crystal Structure of Cbpf, a Bifunctional Choline-Binding Protein and Autolysis Regulator from Streptococcus Pneumoniae.
Embo Rep., 10:246-, 2009

PubMed Abstract: Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline-binding proteins. The three-dimensional structure of choline-binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non-consensus choline-binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well-defined modules. The carboxy-terminal module is involved in cell wall binding and the amino-terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis.

PubMed: 19165143
DOI: 10.1038/EMBOR.2008.245

実験手法

X-RAY DIFFRACTION (2.1 Å)