4O5U

Crystal structure of Alkylhydroperoxide Reductase subunit F from E. coli at 2.65 Ang resolution

4O5U の概要

• エントリーDOI: 10.2210/pdb4o5u/pdb
• 関連するPDBエントリー: 1FL2 4o5q 4o5r
• 分子名称: Alkyl hydroperoxide reductase subunit F, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57909.34

構造登録者

Kamariah, N.,Dip, P.V.,Manimekalai, M.S.S.,Gruber, G.,Eisenhaber, F.,Eisenhaber, B. (登録日: 2013-12-20, 公開日: 2014-11-05, 最終更新日: 2024-11-06)

主引用文献

Dip, P.V.,Kamariah, N.,Subramanian Manimekalai, M.S.,Nartey, W.,Balakrishna, A.M.,Eisenhaber, F.,Eisenhaber, B.,Gruber, G.
Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli
Acta Crystallogr.,Sect.D, 70:2848-2862, 2014

PubMed Abstract: Hydroperoxides are reactive oxygen species (ROS) that are toxic to all cells and must be converted into the corresponding alcohols to alleviate oxidative stress. In Escherichia coli, the enzyme primarily responsible for this reaction is alkylhydroperoxide reductase (AhpR). Here, the crystal structures of both of the subunits of EcAhpR, EcAhpF (57 kDa) and EcAhpC (21 kDa), have been solved. The EcAhpF structures (2.0 and 2.65 Å resolution) reveal an open and elongated conformation, while that of EcAhpC (3.3 Å resolution) forms a decameric ring. Solution X-ray scattering analysis of EcAhpF unravels the flexibility of its N-terminal domain, and its binding to EcAhpC was demonstrated by isothermal titration calorimetry. These studies suggest a novel overall mechanistic model of AhpR as a hydroperoxide scavenger, in which the dimeric, extended AhpF prefers complex formation with the AhpC ring to accelerate the catalytic activity and thus to increase the chance of rescuing the cell from ROS.

PubMed: 25372677
DOI: 10.1107/S1399004714019233

実験手法

X-RAY DIFFRACTION (2.65 Å)