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Journal of Bacteriology, July 2003, p. 4280-4284, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4280-4284.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Crystal Structures of Mycobacterium smegmatis RecA and Its Nucleotide Complexes

S. Datta,1 R. Krishna,1 N. Ganesh,2 Nagasuma R. Chandra,3 K. Muniyappa,2 and M. Vijayan1*

Molecular Biophysics Unit,1 Department of Biochemistry,2 Bioinformatics Centre, Indian Institute of Science, Bangalore 560 012, India3

Received 28 January 2003/ Accepted 22 April 2003

The crystal structures of Mycobacterium smegmatis RecA (RecAMs) and its complexes with ADP, ATP{gamma}S, and dATP show that RecAMs has an expanded binding site like that in Mycobacterium tuberculosis RecA, although there are small differences between the proteins in their modes of nucleotide binding. Nucleotide binding is invariably accompanied by the movement of Gln 196, which appears to provide the trigger for transmitting the effect of nucleotide binding to the DNA-binding loops. These observations provide a framework for exploring the known properties of the RecA proteins.

* Corresponding author. Mailing address: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India. Phone: 91 80 3600765. Fax: 91 80 3600535/683. E-mail: mv{at}mbu.iisc.ernet.in.

Journal of Bacteriology, July 2003, p. 4280-4284, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4280-4284.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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