6T9M
Crystal structure of the Chitinase Domain of the Spore Coat Protein CotE from Clostridium difficile
これはPDB形式変換不可エントリーです。
6T9M の概要
エントリーDOI | 10.2210/pdb6t9m/pdb |
分子名称 | Peroxiredoxin, Peptide in active site, PENTAETHYLENE GLYCOL, ... (5 entities in total) |
機能のキーワード | spore coat, chitinase, colonisation factor, structural protein |
由来する生物種 | Peptoclostridium difficile (strain 630) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 44222.56 |
構造登録者 | Whittingham, J.L.,Dodson, E.J.,Wilkinson, A.J. (登録日: 2019-10-28, 公開日: 2020-07-22, 最終更新日: 2024-11-06) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.3 Å) |
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