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| Subject Categories: Genome Stability & Dynamics | Structural Biology |
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| The EMBO Journal
(2006) 25, 398–408, doi:10.1038/sj.emboj.7600922 Published online 5 January 2006 |
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| Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases |
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| Bhupesh Taneja1, Asmita Patel1, Alexei Slesarev2 and Alfonso Mondragón1 |
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1 Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL, USA 2 Fidelity Systems Inc., Gaithersburg, MD, USA To whom correspondence should be addressed Alfonso Mondragón, Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, IL 60208-3500, USA. Tel.: +1 847 491 7726; Fax: +1 847 467 6489; E-mail: a-mondragon@northwestern.edu Received 3 June 2005; Accepted 23 November 2005; Published online 5 January 2006. |
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| Abstract |
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| Topoisomerases are involved in controlling and maintaining the topology of DNA and are present in all kingdoms of life. Unlike all other types of topoisomerases, similar type IB enzymes have only been identified in bacteria and eukarya. The only putative type IB topoisomerase in archaea is represented by Methanopyrus kandleri topoisomerase V. Despite several common functional characteristics, topoisomerase V shows no sequence similarity to other members of the same type. The structure of the 61 kDa N-terminal fragment of topoisomerase V reveals no structural similarity to other topoisomerases. Furthermore, the structure of the active site region is different, suggesting no conservation in the cleavage and religation mechanism. Additionally, the active site is buried, indicating the need of a conformational change for activity. The presence of a topoisomerase in archaea with a unique structure suggests the evolution of a separate mechanism to alter DNA. |
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| Keywords: helix–hairpin–helix motif, helix–turn–helix domain, Methanopyrus kandleri, topoisomerase IB, topoisomerase V |
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