Abstract
The DNA topoisomerases are fascinating, ubiquitous, essential enzymes that perform remarkable contortions on DNA [1] .There are two main classes, depending on the DNA substrate: the type I and type II topoisomerases, which operate on single-stranded and duplex DNA respectively. The type II topoisomerases also differ in that they have a requirement for ATP. The reaction involves enzymatic cleavage of DNA (forming an enzyme/cleaved-DNA complex), the translocation of another portion of DNA through the break, followed by religation of the cleaved DNA. As a result of this enzyme reaction, DNA may become supercoiled or relaxed, catenated or decatenated. Such reactions are involved in a number of critical cellular processes, such as transcription, replication and recombination. Topoisomerases I, III and V belong to the type I topoisomerases while topoisomerases II, IV and gyrase belong to the type II class. The type I proteins exist as a single polypeptide, while those of the type II class are oligomeric. The crystal structure of a 67kDa N-terminal fragment of E. coli topoisomerase I shows that this portion of the polypeptide monomer contains four domains that form a circle, which is thought to open and close during catalysis [2]. Topoisomerase I differs from topoisomerases III and V in its dependence on magnesium ions for activity.
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© 1998 Springer Science+Business Media Dordrecht
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Pauptit, R. et al. (1998). Antibacterial Design Based on the Structures of Gyrase-Inhibitor Complexes. In: Codding, P.W. (eds) Structure-Based Drug Design. NATO ASI Series, vol 352. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9028-0_23
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DOI: https://doi.org/10.1007/978-94-015-9028-0_23
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