TY - JOUR
T1 - Flexibility at Gly-194 Is Required for DNA Cleavage and Relaxation Activity of Escherichia coli DNA Topoisomerase I
AU - Cheng, Bokun
AU - Feng, Jingyang
AU - Gadgil, Sharvari
AU - Tse-Dinh, Yuk Ching
PY - 2004/3/5
Y1 - 2004/3/5
N2 - The proposed mechanism of type IA DNA topoisomerase I includes conformational changes by the single enzyme polypeptide to allow binding of the G strand of the DNA substrate at the active site, and the opening or closing of the "gate" created on the G strand of DNA to the passing single or double DNA strand(s) through the cleaved G strand DNA. The shifting of an α helix upon G strand DNA binding has been observed from the comparison of the type IA DNA topoisomerase crystal structures (Changela, A., DiGate, R. J., and Mondragón, A. (2001) Nature 411, 1077-1081). Site-directed mutagenesis of the strictly conserved Gly-194 at the N terminus of this a helix in Escherichia coli DNA topoisomerase I showed that flexibility around this glycine residue is required for DNA cleavage and relaxation activity and supports a functional role for this hinge region in the enzyme conformational change.
AB - The proposed mechanism of type IA DNA topoisomerase I includes conformational changes by the single enzyme polypeptide to allow binding of the G strand of the DNA substrate at the active site, and the opening or closing of the "gate" created on the G strand of DNA to the passing single or double DNA strand(s) through the cleaved G strand DNA. The shifting of an α helix upon G strand DNA binding has been observed from the comparison of the type IA DNA topoisomerase crystal structures (Changela, A., DiGate, R. J., and Mondragón, A. (2001) Nature 411, 1077-1081). Site-directed mutagenesis of the strictly conserved Gly-194 at the N terminus of this a helix in Escherichia coli DNA topoisomerase I showed that flexibility around this glycine residue is required for DNA cleavage and relaxation activity and supports a functional role for this hinge region in the enzyme conformational change.
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U2 - 10.1074/jbc.M312095200
DO - 10.1074/jbc.M312095200
M3 - Article
C2 - 14711811
AN - SCOPUS:1542275519
SN - 0021-9258
VL - 279
SP - 8648
EP - 8654
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 10
ER -