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| {{STRUCTURE_1mx0| PDB=1mx0 | SCENE= }} | | {{STRUCTURE_1mx0| PDB=1mx0 | SCENE= }} |
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| '''Structure of topoisomerase subunit'''
| | ===Structure of topoisomerase subunit=== |
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| ==Overview==
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| Type IIA and type IIB topoisomerases each possess the ability to pass one DNA duplex through another in an ATP-dependent manner. The role of ATP in the strand passage reaction is poorly understood, particularly for the type IIB (topoisomerase VI) family. We have solved the structure of the ATP-binding subunit of topoisomerase VI (topoVI-B) in two states: an unliganded monomer and a nucleotide-bound dimer. We find that topoVI-B is highly structurally homologous to the entire 40-43 kDa ATPase region of type IIA topoisomerases and MutL proteins. Nucleotide binding to topoVI-B leads to dimerization of the protein and causes dramatic conformational changes within each protomer. Our data demonstrate that type IIA and type IIB topoisomerases have descended from a common ancestor and reveal how ATP turnover generates structural signals in the reactions of both type II topoisomerase families. When combined with the structure of the A subunit to create a picture of the intact topoisomerase VI holoenzyme, the ATP-driven motions of topoVI-B reveal a simple mechanism for strand passage by the type IIB topoisomerases.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12505993}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12505993 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12505993}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ghkl atpase]] | | [[Category: Ghkl atpase]] |
| [[Category: Topoisomerase]] | | [[Category: Topoisomerase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:49:17 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:37:18 2008'' |
