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in complex with NADH, to 2.5 A resolution. The asymmetric unit contains a tetramer of tight dimers. Structure does not contain a cofactor-binding domain with Rossmann-fold topology. The NADH is bound in an extended conformation in each active site, in a manner that explains the pro-S specificity. Cofactor binding involves residues belonging to both subunits within the tight dimers. The results indicate the existence of a substrate discrimination mechanism, which involves electrostatic interactions
recombinant enzyme is crystallized with ammonium sulfate as precipitant in the presence of NAD+. The crystals belong to the trigonal space group P3(2)21, with a = 135.9 A and c = 205.9 A, and diffract X-rays to 2.2 A resolution