8Q4E

Structure of Legionella pneumophila Lcl C-terminal domain

8Q4E の概要

• エントリーDOI: 10.2210/pdb8q4e/pdb
• 分子名称: HbP1 (2 entities in total)
• 機能のキーワード: lcl, t2ss, adhesion, biofilm, legionella pneumophila, collagen, cell adhesion
• 由来する生物種: Legionella pneumophila 130b
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 56421.18

構造登録者

Rehman, S.,Garnett, J.A. (登録日: 2023-08-06, 公開日: 2023-12-27, 最終更新日: 2024-11-06)

主引用文献

Rehman, S.,Antonovic, A.K.,McIntire, I.E.,Zheng, H.,Cleaver, L.,Adams, C.O.,Portlock, T.,Richardson, K.,Shaw, R.,Oregioni, A.,Mastroianni, G.,Whittaker, S.B.,Kelly, G.,Fornili, A.,Cianciotto, N.P.,Garnett, J.A.
The Legionella collagen-like protein employs a unique binding mechanism for the recognition of host glycosaminoglycans.
Biorxiv, 2023

PubMed Abstract: Bacterial adhesion is a fundamental process which enables colonisation of niche environments and is key for infection. However, in , the causative agent of Legionnaires' disease, these processes are not well understood. The collagen-like protein (Lcl) is an extracellular peripheral membrane protein that recognises sulphated glycosaminoglycans (GAGs) on the surface of eukaryotic cells, but also stimulates bacterial aggregation in response to divalent cations. Here we report the crystal structure of the Lcl C-terminal domain (Lcl-CTD) and present a model for intact Lcl. Our data reveal that Lcl-CTD forms an unusual dynamic trimer arrangement with a positively charged external surface and a negatively charged solvent exposed internal cavity. Through Molecular Dynamics (MD) simulations, we show how the GAG chondroitin-4-sulphate associates with the Lcl-CTD surface via unique binding modes. Our findings show that Lcl homologs are present across both the Pseudomonadota and Fibrobacterota-Chlorobiota-Bacteroidota phyla and suggest that Lcl may represent a versatile carbohydrate binding mechanism.

PubMed: 38106198
DOI: 10.1101/2023.12.10.570962

実験手法

X-RAY DIFFRACTION (1.9 Å)