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5ZDP

Crystal structure of cyanide-insensitive alternative oxidase from Trypanosoma brucei with ferulenol

5ZDP の概要
エントリーDOI10.2210/pdb5zdp/pdb
分子名称Alternative oxidase, mitochondrial, FE (III) ION, HYDROXIDE ION, ... (6 entities in total)
機能のキーワードmembrane bound diiron protein, membrane protein
由来する生物種Trypanosoma brucei brucei
タンパク質・核酸の鎖数4
化学式量合計152681.91
構造登録者
主引用文献Shiba, T.,Inaoka, D.K.,Takahashi, G.,Tsuge, C.,Kido, Y.,Young, L.,Ueda, S.,Balogun, E.O.,Nara, T.,Honma, T.,Tanaka, A.,Inoue, M.,Saimoto, H.,Harada, S.,Moore, A.L.,Kita, K.
Insights into the ubiquinol/dioxygen binding and proton relay pathways of the alternative oxidase.
Biochim Biophys Acta Bioenerg, 1860:375-382, 2019
Cited by
PubMed Abstract: The alternative oxidase (AOX) is a monotopic diiron carboxylate protein which catalyzes the four-electron reduction of dioxygen to water by ubiquinol. Although we have recently determined the crystal structure of Trypanosoma brucei AOX (TAO) in the presence and absence of ascofuranone (AF) derivatives (which are potent mixed type inhibitors) the mechanism by which ubiquinol and dioxygen binds to TAO remain inconclusive. In this article, ferulenol was identified as the first competitive inhibitor of AOX which has been used to probe the binding of ubiquinol. Surface plasmon resonance reveals that AF is a quasi-irreversible inhibitor of TAO whilst ferulenol binding is completely reversible. The structure of the TAO-ferulenol complex, determined at 2.7 Å, provided insights into ubiquinol binding and has also identified a potential dioxygen molecule bound in a side-on conformation to the diiron center for the first time.
PubMed: 30910528
DOI: 10.1016/j.bbabio.2019.03.008
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.71 Å)
構造検証レポート
Validation report summary of 5zdp
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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