2WXT
Clostridium perfringens alpha-toxin strain NCTC8237
2WXT の概要
| エントリーDOI | 10.2210/pdb2wxt/pdb |
| 関連するPDBエントリー | 1QM6 1QMD 2WXU 2WY6 |
| 分子名称 | PHOSPHOLIPASE C, ZINC ION, CADMIUM ION, ... (5 entities in total) |
| 機能のキーワード | cytolysis, hydrolase, hemolysis, membrane binding, gangrene determinant, c2 domain, virulence |
| 由来する生物種 | CLOSTRIDIUM PERFRINGENS |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 43622.67 |
| 構造登録者 | |
| 主引用文献 | Vachieri, S.G.,Clark, G.C.,Alape-Giron, A.,Flores-Diaz, M.,Justin, N.,Naylor, C.E.,Titball, R.W.,Basak, A.K. Comparison of a Nontoxic Variant of Clostridium Perfringens [Alpha]-Toxin with the Toxic Wild-Type Strain Acta Crystallogr.,Sect.D, 66:1067-, 2010 Cited by PubMed Abstract: The α-toxin produced by Clostridium perfringens is one of the best-studied examples of a toxic phospholipase C. In this study, a nontoxic mutant protein from C. perfringens strain NCTC8237 in which Thr74 is substituted by isoleucine (T74I) has been characterized and is compared with the toxic wild-type protein. Thr74 is part of an exposed loop at the proposed membrane-interfacing surface of the toxin. The mutant protein had markedly reduced cytotoxic and myotoxic activities. However, this substitution did not significantly affect the catalytic activity towards water-soluble substrate or the overall three-dimensional structure of the protein. The data support the proposed role of the 70-90 loop in the recognition of membrane phospholipids. These findings also provide key evidence in support of the hypothesis that the hydrolysis of both phosphatidylcholine and sphingomyelin are required for the cytolytic and toxic activity of phospholipases. PubMed: 20944240DOI: 10.1107/S090744491003369X 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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