Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes

被引：51

作者：

Datta, S

Krishna, R

Ganesh, N

Chandra, NR

Muniyappa, K

Vijayan, M ^{[1
]}

机构：

[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India

[2] Indian Inst Sci, Dept Biochem, Bangalore 560012, Karnataka, India

[3] Indian Inst Sci, Bioinformat Ctr, Bangalore 560012, Karnataka, India

来源：

JOURNAL OF BACTERIOLOGY | 2003年 / 185卷 / 14期

关键词：

D O I：

10.1128/JB.185.14.4280-4284.2003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：4280 / 4284

页数：5

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