4G09
The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone
Summary for 4G09
| Entry DOI | 10.2210/pdb4g09/pdb |
| Related | 4G07 |
| Descriptor | Histidinol dehydrogenase, ZINC ION, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | rossmann fold, l-histidinol dehydrogenase, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Brucella suis |
| Total number of polymer chains | 1 |
| Total formula weight | 47816.73 |
| Authors | D'Ambrosio, K.,De Simone, G. (deposition date: 2012-07-09, release date: 2013-10-02, Last modification date: 2024-02-28) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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