1GU7

Enoyl thioester reductase from Candida tropicalis

1GU7 の概要

• エントリーDOI: 10.2210/pdb1gu7/pdb
• 関連するPDBエントリー: 1GUF 1GYR
• 分子名称: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADPH, B-SPECIFIC] 1,MITOCHONDRIAL, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, thioester reduction, fatty acids
• 由来する生物種: CANDIDA TROPICALIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81188.47

構造登録者

Airenne, T.T.,Torkko, J.M.,Wierenga, R.K.,Hiltunen, J.K. (登録日: 2002-01-24, 公開日: 2003-03-13, 最終更新日: 2024-05-08)

主引用文献

Airenne, T.T.,Torkko, J.M.,Van Der Plas, S.,Sormunen, R.T.,Kastaniotis, A.J.,Wierenga, R.K.,Hiltunen, J.K.
Structure-Function Analysis of Enoyl Thioester Reductase Involved in Mitochondrial Maintenance
J.Mol.Biol., 327:47-, 2003

PubMed Abstract: Candida tropicalis enoyl thioester reductase Etr1p and the Saccharomyces cerevisiae homologue Mrf1p catalyse the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (FAS). Unlike prokaryotic enoyl thioester reductases (ETRs), which belong to the short-chain dehydrogenases/reductases (SDR), Etr1p and Mrf1p represent structurally distinguishable ETRs that belong to the medium-chain dehydrogenases/reductases (MDR) superfamily, indicating independent origin of two separate classes of ETRs. The crystal structures of Etr1p, the Etr1p-NADPH complex and the Etr1Y79Np mutant were refined to 1.70A, 2.25A and 2.60A resolution, respectively. The native fold of Etr1p was maintained in Etr1Y79Np, but the mutant had only 0.1% of Etr1p catalytic activity remaining and failed to rescue the respiratory deficient phenotype of the mrf1Delta strain. Mutagenesis of Tyr73 in Mrf1p, corresponding to Tyr79 in Etr1p, produced similar results. Our data indicate that the mitochondrial reductase activity is indispensable for respiratory function in yeast, emphasizing the significance of Mrf1p (Etr1p) and mitochondrial FAS for the integrity of the respiratory competent organelle.

PubMed: 12614607
DOI: 10.1016/S0022-2836(03)00038-X

実験手法

X-RAY DIFFRACTION (1.7 Å)