7b81 | pdb_00007b81

Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase (NAD bound-form)

spinqualitylabelsall models 7b81, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b81 is a 2 chain structure with sequence from Azovd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAD Gene: Avin_09160 (AZOVD) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Several microorganisms can utilize L-rhamnose as a carbon and energy source through the non-phosphorylative metabolic pathway, in which L-rhamnose 1-dehydrogenase (RhaDH) catalyzes the NAD(P)(+) -dependent oxidization of L-rhamnose to L-rhamnono-1,4-lactone. We herein investigated the crystal structures of RhaDH from Azotobacter vinelandii in ligand-free, NAD(+) -bound, NADP(+) -bound, and L-rhamnose- and NAD(+) -bound forms at 1.9, 2.1, 2.4, and 1.6 A resolution, respectively. The significant interactions with the 2'-phosphate group of NADP(+) , but not the 2'-hydroxyl group of NAD(+) , were consistent with a preference for NADP(+) over NAD(+) . The C5-OH and C6-methyl groups of L-rhamnose were recognized by specific residues of RhaDH through hydrogen bonds and hydrophobic contact, respectively, which contribute to the different substrate specificities from other aldose 1-dehydrogenases in the short-chain dehydrogenase/reductase superfamily. Crystal structure of L-rhamnose 1-dehydrogenase involved in the non-phosphorylative pathway of L-rhamnose metabolism in bacteria.,Yoshiwara K, Watanabe S, Watanabe Y FEBS Lett. 2021 Jan 22. doi: 10.1002/1873-3468.14046. PMID:33482017 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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