1gyr
From Proteopedia
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MUTANT FORM OF ENOYL THIOESTER REDUCTASE FROM CANDIDA TROPICALIS
Overview
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.
About this Structure
1GYR is a Single protein structure of sequence from Candida tropicalis with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance., Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK, J Mol Biol. 2003 Mar 14;327(1):47-59. PMID:12614607
Page seeded by OCA on Sun Feb 3 09:44:06 2008
