6T9M

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 6T9M

• Entry DOI: 10.2210/pdb6t9m/pdb
• Descriptor: Peroxiredoxin, Peptide in active site, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: spore coat, chitinase, colonisation factor, structural protein
• Biological source: Peptoclostridium difficile (strain 630); More
• Total number of polymer chains: 2
• Total formula weight: 44222.56

Authors

Whittingham, J.L.,Dodson, E.J.,Wilkinson, A.J. (deposition date: 2019-10-28, release date: 2020-07-22, Last modification date: 2024-11-06)

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

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: 32510464
DOI: 10.1107/S2053230X20006147

Experimental method

X-RAY DIFFRACTION (1.3 Å)