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8Q4E

Structure of Legionella pneumophila Lcl C-terminal domain

Summary for 8Q4E
Entry DOI10.2210/pdb8q4e/pdb
DescriptorHbP1 (2 entities in total)
Functional Keywordslcl, t2ss, adhesion, biofilm, legionella pneumophila, collagen, cell adhesion
Biological sourceLegionella pneumophila 130b
Total number of polymer chains3
Total formula weight56421.18
Authors
Rehman, S.,Garnett, J.A. (deposition date: 2023-08-06, release date: 2023-12-27, Last modification date: 2024-11-06)
Primary citationRehman, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

227111

数据于2024-11-06公开中

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