1dub

From Proteopedia

Revision as of 12:57, 30 October 2007

2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5

Overview

The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA), hydratase complexed with the potent inhibitor acetoacetyl-CoA has been, refined at 2.5 angstroms resolution. This enzyme catalyses the reversible, addition of water to alpha,beta-unsaturated enoyl-CoA thioesters, with, nearly diffusion-controlled reaction rates for the best substrates., Enoyl-CoA hydratase is a hexamer of six identical subunits of 161 kDa, molecular mass for the complex. The hexamer is a dimer of trimers. The, monomer is folded into a right-handed spiral of four turns, followed by, two small domains which are involved in trimerization. Each turn of the, spiral consists of two beta-strands and an alpha-helix. The mechanism for, the hydratase/dehydratase reaction follows a syn-stereochemistry, a, ... [(full description)]

About this Structure

1DUB is a [Single protein] structure of sequence from [Rattus norvegicus] with CAA as [ligand]. Active as [Enoyl-CoA hydratase], with EC number [4.2.1.17]. Structure known Active Sites: CR1 and CR2. Full crystallographic information is available from [OCA].

Reference

Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket., Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK, EMBO J. 1996 Oct 1;15(19):5135-45. PMID:8895557

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