1o95
From Proteopedia
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TERNARY COMPLEX BETWEEN TRIMETHYLAMINE DEHYDROGENASE AND ELECTRON TRANSFERRING FLAVOPROTEIN
Overview
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.
About this Structure
1O95 is a Protein complex structure of sequences from Methylophilus methylotrophus with , , and as ligands. Active as Transferred entry: 1.5.8.2, with EC number 1.5.99.7 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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