1O95

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

1O95 の概要

• エントリーDOI: 10.2210/pdb1o95/pdb
• 関連するPDBエントリー: 1DJN 1DJQ 1E11 1O94 1O96 1O97 2TMD
• 分子名称: TRIMETHYLAMINE DEHYDROGENASE, ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT, ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT, ... (7 entities in total)
• 機能のキーワード: electron transport-complex, protein complex, electron transfer, dehydrogenase, electron transport, flavoprotein, oxido-reductase, iron-sulfur, fmn
• 由来する生物種: METHYLOPHILUS METHYLOTROPHUS; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 291482.45

構造登録者

Leys, D.,Basran, J.,Talfournier, F.,Sutcliffe, M.J.,Scrutton, N.S. (登録日: 2002-12-11, 公開日: 2003-02-06, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.7 Å)