3nt4 | pdb_00003nt4

Crystal structure of myo-inositol dehydrogenase from Bacillus subtilis with bound cofactor NADH and inositol

spinqualitylabelsall models 3nt4, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nt4 is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: INS, NAI Related: 3mz0, 3nt2, 3nt5, 3ntq, 3ntr Gene: BSU39700, E83G, idh, iolG, NP_391849.2 ("Bacillus globigii" Migula 1900) Activity: Inositol 2-dehydrogenase, with EC number 1.1.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IOLG_BACSU] Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively. Can also use D-glucose and D-xylose, and shows a trace of activity with D-ribose and D-fructose. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Inositol dehydrogenase from Bacillus subtilis (BsIDH) is a NAD+-dependent enzyme that catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose. We have determined the crystal structures of wild type BsIDH and of the inactive K97V mutant in apo-, holo- and ternary complexes with inositol and inosose. BsIDH is a tetramer, with a novel arrangement consisting of 2 long continuous beta-sheets, formed from all 4 monomers, in which the central 2 strands are crossed over to form the core of the tetramer. Each subunit in the tetramer consists of two domains, an N-terminal Rossmann fold domain containing the cofactor-binding site, and a C-terminal domain containing the inositol-binding site. Structural analysis allowed us to determine residues important in cofactor and substrate binding. Lys97, Asp172, and His176 are the catalytic triad involved in the catalytic mechanism of BsIDH similar to what has been proposed for related enzymes and short chain dehydrogenases. Furthermore, a conformational change in the nicotinamide ring was observed in some ternary complexes, suggesting hydride transfer to the si-face of NAD+. Finally, comparison of the structure and sequence of BsIDH with other putative inositol dehydrogenases allowed us to differentiate these enzymes in four sub-families based on 6 consensus sequence motifs defining the cofactor- and substrate-binding sites. Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification.,van Straaten KE, Zheng H, Palmer DR, Sanders DA Biochem J. 2010 Sep 1. PMID:20809899 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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