5x20

The ternary structure of D-mandelate dehydrogenase with NADH and anilino(oxo)acetate

spinqualitylabelsall models 5x20, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x20 is a 6 chain structure with sequence from Enterococcus faecium DO. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: AOT, GOL, NAD, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3Y316_ENTFD Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.[ARBA:ARBA00002919][RuleBase:RU362068] Publication Abstract from PubMed Enterococcus faecium NAD-dependent d-mandelate dehydrogenase (d-ManDH) belongs to a ketopantoate reductase (KPR)-related d-2-hydroxyacid dehydrogenase family, and exhibits broad substrate specificity toward bulky hydrophobic 2-ketoacids, preferring C3-branched substrates. The ternary complex structure of d-ManDH with NADH and anilino(oxo)acetate (AOA) revealed that the substrate binding induces a shear motion of the N-terminal domain along the C-terminal domain, following the hinge motion induced by the NADH binding, and allows the bound NADH molecule to form favorable interactions with a 2-ketoacid substrate. d-ManDH possesses a sufficiently wide pocket that accommodates the C3 branched side chains of substrates like KPR, but unlike the pocket of KPR, the pocket of d-ManDH comprises an entirely hydrophobic surface and an expanded space, in which the AOA benzene is accommodated. The expanded space mostly comprises a mobile loop structure, which likely modulates the shape and size of the space depending on the substrate. The ternary complex structure of d-mandelate dehydrogenase with NADH and anilino(oxo)acetate.,Furukawa N, Miyanaga A, Nakajima M, Taguchi H Biochem Biophys Res Commun. 2017 Mar 19. pii: S0006-291X(17)30552-1. doi:, 10.1016/j.bbrc.2017.03.088. PMID:28327357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mandelate dehydrogenase

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