4CNL

Crystal structure of the Choline-binding domain of CbpL from Streptococcus pneumoniae

4CNL の概要

• エントリーDOI: 10.2210/pdb4cnl/pdb
• 分子名称: PUTATIVE PNEUMOCOCCAL SURFACE PROTEIN, CHOLINE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: choline-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: 22258.52

構造登録者

Gutierrez-Fernandez, J.,Bartual, S.G.,Hermoso, J.A. (登録日: 2014-01-23, 公開日: 2015-02-18, 最終更新日: 2024-05-08)

主引用文献

Gutierrez-Fernandez, J.,Saleh, M.,Alcorlo, M.,Gomez-Mejia, A.,Pantoja-Uceda, D.,Trevino, M.A.,Vos, F.,Abdullah, M.R.,Galan-Bartual, S.,Seinen, J.,Sanchez-Murcia, P.A.,Gago, F.,Bruix, M.,Hammerschmidt, S.,Hermoso, J.A.
Modular Architecture and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L (Cbpl) Contributing to Pneumococcal Pathogenesis.
Sci.Rep., 6:38094-, 2016

PubMed Abstract: The human pathogen Streptococcus pneumoniae is decorated with a special class of surface-proteins known as choline-binding proteins (CBPs) attached to phosphorylcholine (PCho) moieties from cell-wall teichoic acids. By a combination of X-ray crystallography, NMR, molecular dynamics techniques and in vivo virulence and phagocytosis studies, we provide structural information of choline-binding protein L (CbpL) and demonstrate its impact on pneumococcal pathogenesis and immune evasion. CbpL is a very elongated three-module protein composed of (i) an Excalibur Ca-binding domain -reported in this work for the very first time-, (ii) an unprecedented anchorage module showing alternate disposition of canonical and non-canonical choline-binding sites that allows vine-like binding of fully-PCho-substituted teichoic acids (with two choline moieties per unit), and (iii) a Ltp_Lipoprotein domain. Our structural and infection assays indicate an important role of the whole multimodular protein allowing both to locate CbpL at specific places on the cell wall and to interact with host components in order to facilitate pneumococcal lung infection and transmigration from nasopharynx to the lungs and blood. CbpL implication in both resistance against killing by phagocytes and pneumococcal pathogenesis further postulate this surface-protein as relevant among the pathogenic arsenal of the pneumococcus.

PubMed: 27917891
DOI: 10.1038/SREP38094

実験手法

X-RAY DIFFRACTION (1.7 Å)