5GT1

crystal structure of cbpa from L. salivarius REN

5GT1 の概要

• エントリーDOI: 10.2210/pdb5gt1/pdb
• 分子名称: Choline binding protein A, ZINC ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: s-layer proteins, probiotics, choline-binding protein
• 由来する生物種: Lactobacillus salivarius str. Ren
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19132.28

構造登録者

Jiang, L.,Ren, F. (登録日: 2016-08-18, 公開日: 2017-07-19, 最終更新日: 2023-11-08)

主引用文献

Wang, R.,Jiang, L.,Zhang, M.,Zhao, L.,Hao, Y.,Guo, H.,Sang, Y.,Zhang, H.,Ren, F.
The Adhesion of Lactobacillus salivarius REN to a Human Intestinal Epithelial Cell Line Requires S-layer Proteins
Sci Rep, 7:44029-44029, 2017

PubMed Abstract: Lactobacillus salivarius REN, a novel probiotic isolated from Chinese centenarians, can adhere to intestinal epithelial cells and subsequently colonize the host. We show here that the surface-layer protein choline-binding protein A (CbpA) of L. salivarius REN was involved in adherence to the human colorectal adenocarcinoma cell line HT-29. Adhesion of a cbpA deletion mutant was significantly reduced compared with that of wild-type, suggesting that CbpA acts as an adhesin that mediates the interaction between the bacterium and its host. To identify the molecular mechanism of adhesion, we determined the crystal structure of a truncated form of CbpA that is likely involved in binding to its cell-surface receptor. The crystal structure identified CbpA as a peptidase of the M23 family whose members harbor a zinc-dependent catalytic site. Therefore, we propose that CbpA acts as a multifunctional surface protein that cleaves the host extracellular matrix and participates in adherence. Moreover, we identified enolase as the CbpA receptor on the surface of HT-29 cells. The present study reveals a new class of surface-layer proteins as well as the molecular mechanism that may contribute to the ability of L. salivarius REN to colonize the human gut.

PubMed: 28281568
DOI: 10.1038/srep44029

実験手法

X-RAY DIFFRACTION (1.85 Å)