3B6I

WrbA from Escherichia coli, native structure

3B6I の概要

• エントリーDOI: 10.2210/pdb3b6i/pdb
• 関連するPDBエントリー: 3B6J 3B6K 3B6M
• 分子名称: Flavoprotein wrbA, FLAVIN MONONUCLEOTIDE, POLYETHYLENE GLYCOL (N=34), ... (4 entities in total)
• 機能のキーワード: flavoproteins, nadh:quinone oxidoreductase, fmn, flavoprotein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48756.95

構造登録者

Andrade, S.L.A.,Patridge, E.V.,Ferry, J.G.,Einsle, O. (登録日: 2007-10-29, 公開日: 2007-12-11, 最終更新日: 2023-08-30)

主引用文献

Andrade, S.L.,Patridge, E.V.,Ferry, J.G.,Einsle, O.
Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli.
J.Bacteriol., 189:9101-9107, 2007

PubMed Abstract: The flavoprotein WrbA, originally described as a tryptophan (W) repressor-binding protein in Escherichia coli, has recently been shown to exhibit the enzymatic activity of a NADH:quinone oxidoreductase. This finding points toward a possible role in stress response and in the maintenance of a supply of reduced quinone. We have determined the three-dimensional structure of the WrbA holoprotein from E. coli at high resolution (1.66 A), and we observed a characteristic, tetrameric quaternary structure highly similar to the one found in the WrbA homologs of Deinococcus radiodurans and Pseudomonas aeruginosa. A similar tetramer was originally observed in an iron-sulfur flavoprotein involved in the reduction of reactive oxygen species. Together with other, recently characterized proteins such as YhdA or YLR011wp (Lot6p), these tetrameric flavoproteins may constitute a large family with diverse functions in redox catalysis. WrbA binds substrates at an active site that provides an ideal stacking environment for aromatic moieties, while providing a pocket that is structured to stabilize the ADP part of an NADH molecule in its immediate vicinity. Structures of WrbA in complex with benzoquinone and NADH suggest a sequential binding mechanism for both molecules in the catalytic cycle.

PubMed: 17951395
DOI: 10.1128/JB.01336-07

実験手法

X-RAY DIFFRACTION (1.66 Å)