Structural highlights
Function
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS. Extensive conformational sampling in a ternary electron transfer complex. Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:12567183 doi:http://dx.doi.org/10.1038/nsb894
