期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 76, 期 -, 页码 241-249出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X20006147
关键词
Clostridium difficile; spores; CotE; glycosyl hydrolase; 3D domain swapping
资金
- Biotechnology and Biological Sciences Research Council [BB/J007900/1]
- Cross-Boundary Innovation Program of Osaka University
- BBSRC [BB/J007900/1] Funding Source: UKRI
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 beta-barrel fold with a neighbouring subdomain containing a five-stranded beta-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.
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