3CVZ
Structural insights into the molecular organization of the S-layer from Clostridium difficile
Summary for 3CVZ
Entry DOI | 10.2210/pdb3cvz/pdb |
Descriptor | S-layer protein, PHOSPHATE ION, GLYCINE, ... (4 entities in total) |
Functional Keywords | surface layer protein, protein binding, structural protein |
Biological source | Clostridium difficile |
Total number of polymer chains | 4 |
Total formula weight | 116485.34 |
Authors | Albesa-Jove, D.,Fagan, R. (deposition date: 2008-04-20, release date: 2009-03-17, Last modification date: 2024-02-21) |
Primary citation | Fagan, R.P.,Albesa-Jove, D.,Qazi, O.,Svergun, D.I.,Brown, K.A.,Fairweather, N.F. Structural insights into the molecular organization of the S-layer from Clostridium difficile Mol.Microbiol., 71:1308-1322, 2009 Cited by PubMed Abstract: Clostridium difficile expresses a surface layer (S-layer) which coats the surface of the bacterium and acts as an adhesin facilitating interaction of the bacterium with host enteric cells. The S-layer contains a high-molecular-weight S-layer protein (HMW SLP) and its low-molecular-weight partner protein (LMW SLP). We show that these proteins form a tightly associated non-covalent complex, the H/L complex, and we identify the regions of both proteins responsible for complex formation. The 2.4 A X-ray crystal structure of a truncated derivative of the LMW SLP reveals two domains. Domain 1 has a two-layer sandwich architecture while domain 2, predicted to orientate towards the external environment, contains a novel fold. Small-angle X-ray scattering analysis of the H/L complex shows an elongated molecule, with the two SLPs arranged 'end-to-end' interacting with each other through a small contact area. Alignment of LMW SLPs, which exhibit high sequence diversity, reveals a core of conserved residues that could reflect functional conservation, while allowing for immune evasion through sequence variation. These structures are the first described for the S-layer of a bacterial pathogen, and provide insights into the assembly and biogenesis of the S-layer. PubMed: 19183279DOI: 10.1111/j.1365-2958.2009.06603.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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