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 2.51&Aring;" /> '''Human DNA topoisome...)
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'''Human DNA topoisomerase IIa ATPase/ADP'''<br />
'''Human DNA topoisomerase IIa ATPase/ADP'''<br />
==Overview==
==Overview==
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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.
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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==
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1ZXN 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, SO4, ADP and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZXN OCA].
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1ZXN 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>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=GOL:'>GOL</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=1ZXN OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bechis, S.K.]]
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[[Category: Bechis, S K.]]
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[[Category: Ruthenburg, A.J.]]
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[[Category: Ruthenburg, A J.]]
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[[Category: Verdine, G.L.]]
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[[Category: Verdine, G L.]]
[[Category: Wei, H.]]
[[Category: Wei, H.]]
[[Category: ADP]]
[[Category: ADP]]
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[[Category: ghkl nucleotide-binding fold]]
[[Category: ghkl nucleotide-binding fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:42:54 2007''
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''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


1zxn, resolution 2.51Å

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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 , , 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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