The structure of an iron-containing alcohol dehydrogenase from a hyperthermophilic archaeon in two chemical states.

ABSTRACT: An iron-containing alcohol dehydrogenase (FeADH) from the hyperthermophilic archaeon Thermococcus thioreducens was crystallized in unit cells belonging to space groups P2₁, P2₁2₁2₁ and P4₃2₁2, and the crystal structures were solved at 2.4, 2.1 and 1.9 Å resolution, respectively, by molecular replacement using the FeADH from Thermotoga maritima (Schwarzenbacher et al., 2004) as a model. In the monoclinic and orthorhombic crystals the dehydrogenase (molecular mass 41.5 kDa) existed as a dimer containing a twofold noncrystallographic symmetry axis, which was crystallographic in the tetragonal crystals. In the monoclinic and orthorhombic asymmetric units one molecule contained iron and an NADP molecule, while the other did not.

SUBMITTER: Larson SB 

PROVIDER: S-EPMC6450521 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature