2BIB

Crystal structure of the complete modular teichioic acid phosphorylcholine esterase Pce (CbpE) from Streptococcus pneumoniae

2BIB の概要

• エントリーDOI: 10.2210/pdb2bib/pdb
• 分子名称: TEICHOIC ACID PHOSPHORYLCHOLINE ESTERASE/ CHOLINE BINDING PROTEIN, PHOSPHOCHOLINE, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total)
• 機能のキーワード: choline-binding protein, cbpe, pce, phosphorylcholine esterase, hydrolase, teichoic acid
• 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: 65286.88

構造登録者

Hermoso, J.A.,Lagartera, L.,Gonzalez, A.,Garcia, P.,Martinez-Ripoll, M.,Garcia, J.L.,Menendez, M. (登録日: 2005-01-20, 公開日: 2005-05-09, 最終更新日: 2024-05-08)

主引用文献

Hermoso, J.A.,Lagartera, L.,Gonzalez, A.,Stelter, M.,Garcia, P.,Martinez-Ripoll, M.,Garcia, J.L.,Menendez, M.
Insights Into Pneumococcal Pathogenesis from Crystal Structure of the Modular Teichoic Acid Phosphorylcholine Esterase Pce
Nat.Struct.Mol.Biol., 12:533-, 2005

PubMed Abstract: Phosphorylcholine, a specific component of the pneumococcal cell wall, is crucial in pathogenesis. It directly binds to the human platelet-activating factor (PAF) receptor and acts as a docking station for the family of surface-located choline-binding proteins (CBP). The first structure of a complete pneumococcal CBP, Pce (or CbpE), has been solved in complex with the reaction product and choline analogs. Pce has a novel modular structure, with a globular N-terminal module containing a binuclear Zn(2+) catalytic center, and an elongated choline-binding module. Residues involved in substrate binding and catalysis are described and modular configuration of the active center accounts for in vivo features of teichoic acid hydrolysis. The hydrolysis of PAF by Pce and its regulatory role in phosphorylcholine decoration of the bacterial surface provide new insights into the critical function of Pce in pneumococcal adherence and invasiveness.

PubMed: 15895092
DOI: 10.1038/NSMB940

実験手法

X-RAY DIFFRACTION (1.92 Å)