Datta, S and Krishna, R and Ganesh, N and Chandra, Nagasuma R and Muniyappa, K and Vijayan, M (2003) Crystal Structures of Mycobacterium smegmatis RecA and Its Nucleotide Complexes. In: Journal of Bacteriology, 185 . pp. 4280-4284.
The crystal structures of Mycobacterium smegmatis RecA (RecAMs) and its complexes with ADP, ATPS, 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.
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to American Society for Microbiology.|
|Keywords:||mycobacterium smegmatis;nucleotide complexes;dna binding|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Information Sciences > BioInformatics Centre
Division of Biological Sciences > Biochemistry
|Date Deposited:||24 Oct 2004|
|Last Modified:||19 Sep 2010 04:16|
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