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1dub
From Proteopedia
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(New page: 200px<br /> <applet load="1dub" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dub, resolution 2.5Å" /> '''2-ENOYL-COA HYDRATAS...)
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Revision as of 18:57, 29 October 2007
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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 [[1]], with EC number [4.2.1.17]. 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
Page seeded by OCA on Mon Oct 29 21:02:07 2007
