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 - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biochimie Année : 2014

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

Résumé

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.
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hal-02425093 , version 1 (29-12-2019)

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Katia d'Ambrosio, Marie Lopez, Nina Dathan, Safia Ouahrani-Bettache, Stephan Köhler, et al.. 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, 2014, 97, pp.114-120. ⟨10.1016/j.biochi.2013.09.028⟩. ⟨hal-02425093⟩
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