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1dci
From Proteopedia
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DIENOYL-COA ISOMERASE
Overview
BACKGROUND: The degradation of unsaturated fatty acids is vital to all, living organisms. Certain unsaturated fatty acids must be catabolized via, a pathway auxiliary to the main beta-oxidation pathway. Dienoyl-coenzyme A, (dienoyl-CoA) isomerase catalyzes one step of this auxiliary pathway, the, isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, and is imported into both mitochondria and peroxisomes. Dienoyl-CoA, isomerase belongs to a family of CoA-binding proteins that share the, enoyl-CoA hydratase/isomerase sequence motif. RESULTS: The crystal, structure of rat dienoyl-CoA isomerase has been determined at 1.5 A, resolution. The fold closely resembles that of enoyl-CoA hydratase and, 4-chlorobenzoyl-CoA dehalogenase. Dienoyl-CoA isomerase forms hexamers, made ... [(full description)]
About this Structure
1DCI is a [Single protein] structure of sequence from [Rattus norvegicus] with SO4, MG and EDO as [ligands]. Active as [[1]], with EC number [4.2.1.17]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis., Modis Y, Filppula SA, Novikov DK, Norledge B, Hiltunen JK, Wierenga RK, Structure. 1998 Aug 15;6(8):957-70. PMID:9739087
Page seeded by OCA on Mon Oct 29 17:56:32 2007
Categories: Rattus norvegicus | Single protein | Filppula, S.A. | Hiltunen, J.K. | Modis, Y. | Norledge, B. | Novikov, D. | Wierenga, R.K. | EDO | MG | SO4 | Dienoyl-coa isomerase | Lyase
