5jo9

Structural characterization of the thermostable Bradyrhizobium japonicum d-sorbitol dehydrogenase

spinqualitylabelsall models 5jo9, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jo9 is a 1 chain structure with sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.894Å Ligands: PO4, SOR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q89FN7_BRADU Publication Abstract from PubMed Bradyrhizobium japonicum sorbitol dehydrogenase is NADH-dependent and is active at elevated temperatures. The best substrate is D-glucitol (a synonym for D-sorbitol), although L-glucitol is also accepted, giving it particular potential in industrial applications. Crystallization led to a hexagonal crystal form, with crystals diffracting to 2.9 A resolution. In attempts to phase the data, a molecular-replacement solution based upon PDB entry 4nbu (33% identical in sequence to the target) was found. The solution contained one molecule in the asymmetric unit, but a tetramer similar to that found in other short-chain dehydrogenases, including the search model, could be reconstructed by applying crystallographic symmetry operations. The active site contains electron density consistent with D-glucitol and phosphate, but there was not clear evidence for the binding of NADH. In a search for the features that determine the thermostability of the enzyme, the Tm for the orthologue from Rhodobacter sphaeroides, for which the structure was already known, was also determined, and this enzyme proved to be considerably less thermostable. A continuous beta-sheet is formed between two monomers in the tetramer of the B. japonicum enzyme, a feature not generally shared by short-chain dehydrogenases, and which may contribute to thermostability, as may an increased Pro/Gly ratio. Structural characterization of the thermostable Bradyrhizobium japonicumD-sorbitol dehydrogenase.,Fredslund F, Otten H, Gemperlein S, Poulsen JC, Carius Y, Kohring GW, Lo Leggio L Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):846-852. doi:, 10.1107/S2053230X16016927. Epub 2016 Oct 27. PMID:27827356 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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