1jqi

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Revision as of 16:21, 20 November 2007


1jqi, resolution 2.25Å

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Crystal Structure of Rat Short Chain Acyl-CoA Dehydrogenase Complexed With Acetoacetyl-CoA

Overview

The acyl-CoA dehydrogenases are a family of flavin adenine, dinucleotide-containing enzymes that catalyze the first step in the, beta-oxidation of fatty acids and catabolism of some amino acids. They, exhibit high sequence identity and yet are quite specific in their, substrate binding. Short chain acyl-CoA dehydrogenase has maximal activity, toward butyryl-CoA and negligible activity toward substrates longer than, octanoyl-CoA. The crystal structure of rat short chain acyl-CoA, dehydrogenase complexed with the inhibitor acetoacetyl-CoA has been, determined at 2.25 A resolution. Short chain acyl-CoA dehydrogenase is a, homotetramer with a subunit mass of 43 kDa and crystallizes in the space, group P321 with a = 143.61 A and c = 77.46 A. There are two monomers in, the asymmetric unit. The overall structure of short chain acyl-CoA, dehydrogenase is very similar to those of medium chain acyl-CoA, dehydrogenase, isovaleryl-CoA dehydrogenase, and bacterial short chain, acyl-CoA dehydrogenase with a three-domain structure composed of N- and, C-terminal alpha-helical domains separated by a beta-sheet domain., Comparison to other acyl-CoA dehydrogenases has provided additional, insight into the basis of substrate specificity and the nature of the, oxidase activity in this enzyme family. Ten reported pathogenic human, mutations and two polymorphisms have been mapped onto the structure of, short chain acyl-CoA dehydrogenase. None of the mutations directly affect, the binding cavity or intersubunit interactions.

About this Structure

1JQI is a Single protein structure of sequence from Rattus norvegicus with CAA and FAD as ligands. Active as Butyryl-CoA dehydrogenase, with EC number 1.3.99.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases., Battaile KP, Molin-Case J, Paschke R, Wang M, Bennett D, Vockley J, Kim JJ, J Biol Chem. 2002 Apr 5;277(14):12200-7. Epub 2002 Jan 25. PMID:11812788

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