Nucleic Acids Research Advance Access originally published online on December 23, 2008
Nucleic Acids Research 2009 37(3):693-701; doi:10.1093/nar/gkn1009
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Nucleic Acids Research, 2009, Vol. 37, No. 3 693-701
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Structural studies of type I topoisomerases
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, USA
*To whom correspondence should be addressed. Tel: +1 847 491 7726; Fax: +1 847 467 6489; Email: a-mondragon{at}northwestern.edu
Received October 15, 2008. Revised November 3, 2008. Accepted November 3, 2008.
Topoisomerases are ubiquitous proteins found in all three domains of life. They change the topology of DNA via transient breaks on either one or two of the DNA strands to allow passage of another single or double DNA strand through the break. Topoisomerases are classified into two types: type I enzymes cleave one DNA strand and pass either one or two DNA strands through the break before resealing it, while type II molecules cleave both DNA strands in concert and pass another double strand through the break followed by religation of the double strand break. Here we review recent work on the structure of type I enzymes. These structural studies are providing atomic details that, together with the existing wealth of biochemical and biophysical data, are bringing our understanding of the mechanism of action of these enzymes to the atomic level.