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3CVZ

Structural insights into the molecular organization of the S-layer from Clostridium difficile

Summary for 3CVZ
Entry DOI10.2210/pdb3cvz/pdb
DescriptorS-layer protein, PHOSPHATE ION, GLYCINE, ... (4 entities in total)
Functional Keywordssurface layer protein, protein binding, structural protein
Biological sourceClostridium difficile
Total number of polymer chains4
Total formula weight116485.34
Authors
Albesa-Jove, D.,Fagan, R. (deposition date: 2008-04-20, release date: 2009-03-17, Last modification date: 2024-02-21)
Primary citationFagan, 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: 19183279
DOI: 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

239149

數據於2025-07-23公開中

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