4xb2

Hyperthermophilic archaeal homoserine dehydrogenase mutant in complex with NADPH

spinqualitylabelsall models 4xb2, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xb2 is a 2 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: HSE, NA, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O58802_PYRHO Publication Abstract from PubMed NAD(P)-dependent dehydrogenases differ according to their coenzyme preference: some prefer NAD, others NADP, and still others exhibit dual cofactor specificity. The structure of a newly identified archaeal homoserine dehydrogenase showed this enzyme to have a strong preference for NADP. However, NADP did not act as a cofactor with this enzyme, but as a strong inhibitor of NAD-dependent homoserine oxidation. Structural analysis and site-directed mutagenesis showed that the large number of interactions between the cofactor and the enzyme are responsible for the lack of reactivity of the enzyme towards NADP. This observation suggests this enzyme exhibits a new variation on cofactor binding to a dehydrogenase: very strong NADP binding that acts as an obstacle to NAD(P)-dependent dehydrogenase catalytic activity. Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases.,Hayashi J, Inoue S, Kim K, Yoneda K, Kawarabayasi Y, Ohshima T, Sakuraba H Sci Rep. 2015 Jul 8;5:11674. doi: 10.1038/srep11674. PMID:26154028 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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