5J6Q
Cwp8 from Clostridium difficile
Summary for 5J6Q
| Entry DOI | 10.2210/pdb5j6q/pdb |
| Descriptor | Cell wall binding protein cwp8, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | cell wall protein, s-layer, cwb2 domain, toprim fold, cell adhesion |
| Biological source | Peptoclostridium difficile (strain 630) |
| Total number of polymer chains | 1 |
| Total formula weight | 65620.65 |
| Authors | Renko, M.,Usenik, A.,Turk, D. (deposition date: 2016-04-05, release date: 2017-02-08, Last modification date: 2024-05-08) |
| Primary citation | Usenik, A.,Renko, M.,Mihelic, M.,Lindic, N.,Borisek, J.,Perdih, A.,Pretnar, G.,Muller, U.,Turk, D. The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6. Structure, 25:514-521, 2017 Cited by PubMed Abstract: Bacterial cell wall proteins play crucial roles in cell survival, growth, and environmental interactions. In Gram-positive bacteria, cell wall proteins include several types that are non-covalently attached via cell wall binding domains. Of the two conserved surface-layer (S-layer)-anchoring modules composed of three tandem SLH or CWB2 domains, the latter have so far eluded structural insight. The crystal structures of Cwp8 and Cwp6 reveal multi-domain proteins, each containing an embedded CWB2 module. It consists of a triangular trimer of Rossmann-fold CWB2 domains, a feature common to 29 cell wall proteins in Clostridium difficile 630. The structural basis of the intact module fold necessary for its binding to the cell wall is revealed. A comparison with previously reported atomic force microscopy data of S-layers suggests that C. difficile S-layers are complex oligomeric structures, likely composed of several different proteins. PubMed: 28132783DOI: 10.1016/j.str.2016.12.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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