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Title
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Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes.
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Authors
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S.Datta,
R.Krishna,
N.Ganesh,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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J Bacteriol, 2003,
185,
4280-4284.
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PubMed id
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Abstract
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The crystal structures of Mycobacterium smegmatis RecA (RecA(Ms)) and its
complexes with ADP, ATPgammaS, and dATP show that RecA(Ms) 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.
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