1O95

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

Summary for 1O95

• Entry DOI: 10.2210/pdb1o95/pdb
• Related: 1DJN 1DJQ 1E11 1O94 1O96 1O97 2TMD
• Descriptor: TRIMETHYLAMINE DEHYDROGENASE, ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT, ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT, ... (7 entities in total)
• Functional Keywords: electron transport-complex, protein complex, electron transfer, dehydrogenase, electron transport, flavoprotein, oxido-reductase, iron-sulfur, fmn
• Biological source: METHYLOPHILUS METHYLOTROPHUS; More
• Total number of polymer chains: 6
• Total formula weight: 291482.45

Authors

Leys, D.,Basran, J.,Talfournier, F.,Sutcliffe, M.J.,Scrutton, N.S. (deposition date: 2002-12-11, release date: 2003-02-06, Last modification date: 2024-11-06)

Primary citation

Leys, D.,Basran, J.,Talfournier, F.,Sutcliffe, M.J.,Scrutton, N.S.
Extensive Conformational Sampling in a Ternary Electron Transfer Complex.
Nat.Struct.Biol., 10:219-, 2003

PubMed Abstract: 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.

PubMed: 12567183
DOI: 10.1038/NSB894

Experimental method

X-RAY DIFFRACTION (3.7 Å)