Structural characterization of the thermostable Bradyrhizobium japonicumD-sorbitol dehydrogenase.

ABSTRACT: 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 Å 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-gl

SUBMITTER: Fredslund F 

PROVIDER: S-EPMC5101586 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature