Structure and mechanism of DNA topoisomerase II.
The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints. An enzyme with bound DNA can admit a second DNA duplex through one set of jaws, transport it through the cleaved first duplex, and expel it through the other set of jaws.
Berger
J M
JM
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Gamblin
S J
SJ
Harrison
S C
SC
Wang
J C
JC
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D004247:DNA; D000251:Adenosine Triphosphatases; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II