Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate.

ABSTRACT: Two crystal structures of recombinant Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase (Gs6PDH) in complex with the substrate 6-phosphogluconate have been determined at medium resolution. Gs6PDH shares significant sequence identity and structural similarity with the enzymes from Lactococcus lactis, sheep liver and the protozoan parasite Trypanosoma brucei, for which a range of structures have previously been reported. Comparisons indicate that amino-acid sequence conservation is more pronounced in the two domains that contribute to the architecture of the active site, namely the N-terminal and C-terminal domains, compared with the central domain, which is primarily involved in the subunit-subunit associations required to form a stable dimer. The active-site residues are high

SUBMITTER: Cameron S 

PROVIDER: S-EPMC2675582 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature