1zxm
From Proteopedia
(New page: 200px<br /> <applet load="1zxm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zxm, resolution 1.87Å" /> '''Human Topo IIa ATPa...) |
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| - | [[Image:1zxm.gif|left|200px]]<br /> | + | [[Image:1zxm.gif|left|200px]]<br /><applet load="1zxm" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zxm" size=" | + | |
caption="1zxm, resolution 1.87Å" /> | caption="1zxm, resolution 1.87Å" /> | ||
'''Human Topo IIa ATPase/AMP-PNP'''<br /> | '''Human Topo IIa ATPase/AMP-PNP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Type IIA DNA topoisomerases play multiple essential roles in the | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http:// | + | 1ZXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bechis, S | + | [[Category: Bechis, S K.]] |
| - | [[Category: Ruthenburg, A | + | [[Category: Ruthenburg, A J.]] |
| - | [[Category: Verdine, G | + | [[Category: Verdine, G L.]] |
[[Category: Wei, H.]] | [[Category: Wei, H.]] | ||
[[Category: ANP]] | [[Category: ANP]] | ||
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[[Category: ghkl nucleotide-binding fold]] | [[Category: ghkl nucleotide-binding fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:04 2008'' |
Revision as of 14:20, 21 February 2008
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Human Topo IIa ATPase/AMP-PNP
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
1ZXM is a Single protein structure of sequence from Homo sapiens with and 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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