6TSB
Crystal structure of the Chitinase Domain of the Spore Coat Protein CotE from Clostridium difficile
This is a non-PDB format compatible entry.
Summary for 6TSB
| Entry DOI | 10.2210/pdb6tsb/pdb |
| Descriptor | Peroxiredoxin, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | spore coat, chitinase, colonisation factor, structural protein |
| Biological source | Clostridioides difficile (strain 630) |
| Total number of polymer chains | 1 |
| Total formula weight | 40983.90 |
| Authors | Whittingham, J.L.,Dodson, E.J.,Wilkinson, A.J. (deposition date: 2019-12-20, release date: 2020-06-24, Last modification date: 2024-10-16) |
| Primary citation | Whittingham, J.L.,Hanai, S.,Brannigan, J.A.,Ferreira, W.T.,Dodson, E.J.,Turkenburg, J.P.,Cartwright, J.,Cutting, S.M.,Wilkinson, A.J. Crystal structures of the GH18 domain of the bifunctional peroxiredoxin-chitinase CotE from Clostridium difficile. Acta Crystallogr.,Sect.F, 76:241-249, 2020 Cited by PubMed Abstract: CotE is a coat protein that is present in the spores of Clostridium difficile, an obligate anaerobic bacterium and a pathogen that is a leading cause of antibiotic-associated diarrhoea in hospital patients. Spores serve as the agents of disease transmission, and CotE has been implicated in their attachment to the gut epithelium and subsequent colonization of the host. CotE consists of an N-terminal peroxiredoxin domain and a C-terminal chitinase domain. Here, a C-terminal fragment of CotE comprising residues 349-712 has been crystallized and its structure has been determined to reveal a core eight-stranded β-barrel fold with a neighbouring subdomain containing a five-stranded β-sheet. A prominent groove running across the top of the barrel is lined by residues that are conserved in family 18 glycosyl hydrolases and which participate in catalysis. Electron density identified in the groove defines the pentapeptide Gly-Pro-Ala-Met-Lys derived from the N-terminus of the protein following proteolytic cleavage to remove an affinity-purification tag. These observations suggest the possibility of designing peptidomimetics to block C. difficile transmission. PubMed: 32510464DOI: 10.1107/S2053230X20006147 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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