4G09
The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone
4G09 の概要
| エントリーDOI | 10.2210/pdb4g09/pdb |
| 関連するPDBエントリー | 4G07 |
| 分子名称 | Histidinol dehydrogenase, ZINC ION, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | rossmann fold, l-histidinol dehydrogenase, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| 由来する生物種 | Brucella suis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 47816.73 |
| 構造登録者 | |
| 主引用文献 | D'ambrosio, K.,Lopez, M.,Dathan, N.A.,Ouahrani-Bettache, S.,Kohler, S.,Ascione, G.,Monti, S.M.,Winum, J.Y.,De Simone, G. Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis. Biochimie, 97:114-120, 2014 Cited by PubMed Abstract: L-Histidinol dehydrogenase from Brucella suis (BsHDH) is an enzyme involved in the histidine biosynthesis pathway which is absent in mammals, thus representing a very interesting target for the development of anti-Brucella agents. In this paper we report the crystallographic structure of a mutated form of BsHDH both in its unbound form and in complex with a nanomolar inhibitor. These studies provide the first structural background for the rational design of potent HDH inhibitors, thus offering new hints for clinical applications. PubMed: 24140957DOI: 10.1016/j.biochi.2013.09.028 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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