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J. Biol. Chem., Vol. 275, Issue 21, 16183-16190, May 26, 2000
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Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding*

James B. ThodenDagger , Carol Z. Blanchard§, Hazel M. HoldenDagger , and Grover L. Waldrop§

From the Dagger  Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53705 and the § Division of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, Louisiana 70803-1806

Acetyl-CoA carboxylase catalyzes the first committed step in fatty acid synthesis. In Escherichia coli, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. The biotin carboxylase component has served for many years as a paradigm for mechanistic studies devoted toward understanding more complicated biotin-dependent carboxylases. The three-dimensional x-ray structure of an unliganded form of E. coli biotin carboxylase was originally solved in 1994 to 2.4-Å resolution. This study revealed the architecture of the enzyme and demonstrated that the protein belongs to the ATP-grasp superfamily. Here we describe the three-dimensional structure of the E. coli biotin carboxylase complexed with ATP and determined to 2.5-Å resolution. The major conformational change that occurs upon nucleotide binding is a rotation of approximately 45o of one domain relative to the other domains thereby closing off the active site pocket. Key residues involved in binding the nucleotide to the protein include Lys-116, His-236, and Glu-201. The backbone amide groups of Gly-165 and Gly-166 participate in hydrogen bonding interactions with the phosphoryl oxygens of the nucleotide. A comparison of this closed form of biotin carboxylase with carbamoyl-phosphate synthetase is presented.

* This research was supported in part by National Institutes of Health Grants DK47814 (to H. M. H.) and GM51261 (to G. L. W.) and Shared Instrumentation Grant BIR-9317398 from the National Science Foundation.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 structure factors (codes 1DV1 and 1DV2) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

To whom correspondence should be addressed.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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