6JYX

Structure of CbpJ from Streptococcus Pneumoniae TIGR4

6JYX の概要

• エントリーDOI: 10.2210/pdb6jyx/pdb
• 分子名称: Choline binding protein J, CHOLINE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: streptococcus pneumoniae, choline-binding proteins, adhesion, choline-binding protein
• 由来する生物種: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73244.70

構造登録者

Xu, Q.,Zhang, J.W.,Li, Q.,Jiang, Y.L. (登録日: 2019-04-29, 公開日: 2019-06-05, 最終更新日: 2023-11-22)

主引用文献

Xu, Q.,Zhang, J.W.,Chen, Y.,Li, Q.,Jiang, Y.L.
Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae.
Biochem.Biophys.Res.Commun., 514:1192-1197, 2019

PubMed Abstract: The choline-binding proteins play essential roles in pneumococcal colonization and virulence. It has been suggested that the choline-binding protein J (termed CbpJ; encoded by the gene sp_0378) from Streptococcus pneumoniae TIGR4 involves in the colonization in host and contributes to evasion of neutrophil killing. Here we report the 2.0 Å crystal structure of CbpJ in complex with choline. CbpJ consists of an N-terminal putative functional domain (N-domain) followed by a C-terminal choline-binding domain (CBD). The N-domain harbors four degenerated choline-binding repeats (CBRs) that lose the capacity of binding to choline, whereas the CBD is composed of seven typical CBRs. Further functional assays showed that the CBD contributes to the pneumococcal adhesion to human lung epithelial cell A549. These findings provide insights into the pneumococcal pathogenesis and broaden our understanding on the functions of choline-binding proteins.

PubMed: 31104766
DOI: 10.1016/j.bbrc.2019.05.053

実験手法

X-RAY DIFFRACTION (2 Å)