1o95

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

spinqualitylabelsall models 1o95, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1o95 is a 6 chain structure with sequence from Atcc 53528 and Methylophilus methylotrophus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, AMP, FMN, SF4 Related: 1e11, 1djn, 1djq, 1o94, 1o96, 1o97, 2tmd Activity: Trimethylamine dehydrogenase, with EC number 1.5.8.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ETFA_METME] The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). [ETFB_METME] The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Here we report the crystal structures of a ternary electron transfer complex showing extensive motion at the protein interface. This physiological complex comprises the iron-sulfur flavoprotein trimethylamine dehydrogenase and electron transferring flavoprotein (ETF) from Methylophilus methylotrophus. In addition, we report the crystal structure of free ETF. In the complex, electron density for the FAD domain of ETF is absent, indicating high mobility. Positions for the FAD domain are revealed by molecular dynamics simulation, consistent with crystal structures and kinetic data. A dual interaction of ETF with trimethylamine dehydrogenase provides for dynamical motion at the protein interface: one site acts as an anchor, thereby allowing the other site to sample a large range of interactions, some compatible with rapid electron transfer. This study establishes the role of conformational sampling in multi-domain redox systems, providing insight into electron transfer between ETFs and structurally distinct redox partners. Extensive conformational sampling in a ternary electron transfer complex.,Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:12567183 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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