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Originally published In Press as doi:10.1074/jbc.M111296200 on January 25, 2002

J. Biol. Chem., Vol. 277, Issue 14, 12200-12207, April 5, 2002
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Crystal Structure of Rat Short Chain Acyl-CoA Dehydrogenase Complexed with Acetoacetyl-CoA
COMPARISON WITH OTHER ACYL-CoA DEHYDROGENASES*

Kevin P. BattaileDagger §, JoAnn Molin-CaseDagger §, Rosemary PaschkeDagger , Ming WangDagger , Dennis BennettDagger , Jerry Vockley||, and Jung-Ja P. KimDagger **

From the Dagger  Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226 and || Departments of Biochemistry and Molecular Biology and Medical Genetics, Mayo Clinic and Foundation, Rochester, Minnesota 55905

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 Å 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 Å and c = 77.46 Å. 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.

* This work was supported by Grants GM29076 (to J.-J. P .K.) and DK54936 (to J. V.) from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1JQI) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ These authors contributed equally to this work.

Current address: Dept. of Chemistry, University of Wisconsin- Milwaukee, 3210 N. Cramer St., Milwaukee, WI, 53211.

** To whom correspondence should be addressed: Dept. of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Rd., Milwaukee, WI 53226. Tel.: 414-456-8479; Fax: 414-456-6510; E-mail: jjkim@mcw.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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