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Mol Microbiol. 2005 Oct;58(2):358-66.

Structure and mechanism of Escherichia coli RecA ATPase.

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1
Department of Molecular and Cellular Biochemistry, Ohio State University College of Medicine and Public Health, 371 Hamilton Hall, 1645 Neil Avenue, Columbus, OH 43210, USA. bell.489@osu.edu

Abstract

RecA protein catalyses an ATP-dependent DNA strand-exchange reaction that is the central step in the repair of dsDNA breaks by homologous recombination. Although much is known about the structure of RecA protein itself, we do not at present have a detailed picture of how RecA binds to ssDNA and dsDNA substrates, and how these interactions are controlled by the binding and hydrolysis of the ATP cofactor. Recent studies from electron microscopy and X-ray crystallography have revealed important ATP-mediated conformational changes that occur within the protein, providing new insights into how RecA catalyses DNA strand-exchange. A unifying theme is emerging for RecA and related ATPase enzymes in which the binding of ATP at a subunit interface results in large conformational changes that are coupled to interactions with the substrates in such a way as to promote the desired reactions.

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