1zxn
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(New page: 200px<br /> <applet load="1zxn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zxn, resolution 2.51Å" /> '''Human DNA topoisome...)
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Revision as of 18:36, 12 November 2007
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Human DNA topoisomerase IIa ATPase/ADP
Contents |
Overview
Type IIA DNA topoisomerases play multiple essential roles in the, management of higher-order DNA structure, including modulation of, topological state, chromosome segregation, and chromatin condensation., These diverse physiologic functions are all accomplished through a common, molecular mechanism, wherein the protein catalyzes transient cleavage of a, DNA duplex (the G-segment) to yield a double-stranded gap through which, another duplex (the T-segment) is passed. The overall process is, orchestrated by the opening and closing of molecular "gates" in the, topoisomerase structure, which is regulated by ATP binding, hydrolysis, and release of ADP and inorganic phosphate. Here we present two crystal, structures of the ATPase domain of human DNA topoisomerase IIalpha in, different nucleotide-bound states. Comparison of these structures revealed, rigid-body movement of the structural modules within the ATPase domain, suggestive of the motions of a molecular gate.
Disease
Known diseases associated with this structure: DNA topoisomerase II, resistance to inhibition of, by amsacrine OMIM:[126430]
About this Structure
1ZXN is a Single protein structure of sequence from Homo sapiens with MG, SO4, ADP and GOL as ligands. Active as DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 Full crystallographic information is available from OCA.
Reference
Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase., Wei H, Ruthenburg AJ, Bechis SK, Verdine GL, J Biol Chem. 2005 Nov 4;280(44):37041-7. Epub 2005 Aug 12. PMID:16100112
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