Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution.

摘要: The three-dimensional structure of trimethylamine dehydrogenase from the methylotrophic bacterium W3A1 has been determined to 2.4-A resolution. enzyme is composed two identical 83,000-dalton subunits, each which folded into three structural domains. largest domain, at NH2 terminus molecule, as an eight-stranded parallel alpha/beta barrel. It contains [4Fe-4S] and covalently bound FMN cofactors separated by about 4 A. folding topology large domain orientation cofactor are very similar those found in glycolate oxidase. other domains contain beta sheet topologies with patterns. spatial arrangements these remarkably FAD- NADPH-binding glutathione reductase.