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2dub
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(New page: 200px<br /> <applet load="2dub" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dub, resolution 2.4Å" /> '''ENOYL-COA HYDRATASE ...)
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Revision as of 18:57, 29 October 2007
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ENOYL-COA HYDRATASE COMPLEXED WITH OCTANOYL-COA
Overview
The structure of the hexameric rat mitochondrial enoyl-Coenzyme A (CoA), hydratase, co-crystallised with the inhibitor octanoyl-CoA, has been, refined at a resolution of 2.4 A. Enoyl-CoA hydratase catalyses the, hydration of 2,3-unsaturated enoyl-CoA thioesters. In the crystal, structure only four of the six active sites of the hexamer in the, asymmetric unit are occupied with a ligand molecule, showing an unliganded, and a liganded active site within the same crystal form. While the protein, assembly and fold is identical to the previously solved acetoacetyl-CoA, complex, differences are observed close to the fatty acid binding pocket, due to the different nature of the ligands. The fatty acid tail of, octanoyl-CoA is bound in an extended conformation. This is possible, because a high ... [(full description)]
About this Structure
2DUB is a [Single protein] structure of sequence from [Rattus norvegicus] with CO8 as [ligand]. Active as [[1]], with EC number [4.2.1.17]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule., Engel CK, Kiema TR, Hiltunen JK, Wierenga RK, J Mol Biol. 1998 Feb 6;275(5):847-59. PMID:9480773
Page seeded by OCA on Mon Oct 29 21:02:11 2007
