4g09 | pdb_00004g09

The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone

spinqualitylabelsall models 4g09, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g09 is a 1 chain structure with sequence from Brucella suis 1330. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 0VD, DMS, GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HISX_BRUSU Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity). Publication Abstract from PubMed 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. 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.,D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Kohler S, Ascione G, Monti SM, Winum JY, De Simone G Biochimie. 2013 Oct 17. pii: S0300-9084(13)00349-0. doi:, 10.1016/j.biochi.2013.09.028. PMID:24140957 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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