4G07

The crystal structure of the C366S mutant of HDH from Brucella suis

Summary for 4G07

• Entry DOI: 10.2210/pdb4g07/pdb
• Related: 4G09
• Descriptor: Histidinol dehydrogenase, GLYCEROL, ZINC ION, ... (4 entities in total)
• Functional Keywords: rossmann fold, l-histidinol dehydrogenase, oxidoreductase
• Biological source: Brucella suis 1330
• Total number of polymer chains: 1
• Total formula weight: 47403.20

Authors

D'Ambrosio, K.,De Simone, G. (deposition date: 2012-07-09, release date: 2013-09-04, Last modification date: 2023-09-13)

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

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: 24140957
DOI: 10.1016/j.biochi.2013.09.028

Experimental method

X-RAY DIFFRACTION (1.95 Å)