2A1U

Crystal structure of the human ETF E165betaA mutant

2A1U の概要

• エントリーDOI: 10.2210/pdb2a1u/pdb
• 関連するPDBエントリー: 1EFV 1T9G 2A1T
• 分子名称: Electron transfer flavoprotein alpha-subunit, mitochondrial precursor, Electron transfer flavoprotein beta-subunit, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: electron transfer, mobile domain, conformational sampling, electron transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64081.89

構造登録者

Toogood, H.S.,Van Thiel, A.,Scrutton, N.S.,Leys, D. (登録日: 2005-06-21, 公開日: 2005-07-05, 最終更新日: 2023-10-25)

主引用文献

Toogood, H.S.,van Thiel, A.,Scrutton, N.S.,Leys, D.
Stabilization of Non-productive Conformations Underpins Rapid Electron Transfer to Electron-transferring Flavoprotein
J.Biol.Chem., 280:30361-30366, 2005

PubMed Abstract: Crystal structures of protein complexes with electron-transferring flavoprotein (ETF) have revealed a dual protein-protein interface with one region serving as anchor while the ETF FAD domain samples available space within the complex. We show that mutation of the conserved Glu-165beta in human ETF leads to drastically modulated rates of interprotein electron transfer with both medium chain acyl-CoA dehydrogenase and dimethylglycine dehydrogenase. The crystal structure of free E165betaA ETF is essentially identical to that of wild-type ETF, but the crystal structure of the E165betaA ETF.medium chain acyl-CoA dehydrogenase complex reveals clear electron density for the FAD domain in a position optimal for fast interprotein electron transfer. Based on our observations, we present a dynamic multistate model for conformational sampling that for the wild-type ETF. medium chain acyl-CoA dehydrogenase complex involves random motion between three distinct positions for the ETF FAD domain. ETF Glu-165beta plays a key role in stabilizing positions incompatible with fast interprotein electron transfer, thus ensuring high rates of complex dissociation.

PubMed: 15975918
DOI: 10.1074/jbc.M505562200

実験手法

X-RAY DIFFRACTION (2.11 Å)