8Q4E
Structure of Legionella pneumophila Lcl C-terminal domain
Summary for 8Q4E
Entry DOI | 10.2210/pdb8q4e/pdb |
Descriptor | HbP1 (2 entities in total) |
Functional Keywords | lcl, t2ss, adhesion, biofilm, legionella pneumophila, collagen, cell adhesion |
Biological source | Legionella pneumophila 130b |
Total number of polymer chains | 3 |
Total formula weight | 56421.18 |
Authors | Rehman, S.,Garnett, J.A. (deposition date: 2023-08-06, release date: 2023-12-27, Last modification date: 2024-11-06) |
Primary citation | 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 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: 38106198DOI: 10.1101/2023.12.10.570962 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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