1gyr

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Image:1gyr.gif

1gyr, resolution 2.6Å

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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 ... [(full description)]

About this Structure

1GYR is a [Single protein] structure of sequence from [Candida tropicalis] with SO4 and GOL as [ligands]. Structure known Active Site: GA1. 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

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