1zxn
From Proteopedia
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|PDB= 1zxn |SIZE=350|CAPTION= <scene name='initialview01'>1zxn</scene>, resolution 2.51Å | |PDB= 1zxn |SIZE=350|CAPTION= <scene name='initialview01'>1zxn</scene>, resolution 2.51Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= TOP2A, TOP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= TOP2A, TOP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1zxm|1ZXM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxn OCA], [http://www.ebi.ac.uk/pdbsum/1zxn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zxn RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=126430 126430]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Verdine, G L.]] | [[Category: Verdine, G L.]] | ||
[[Category: Wei, H.]] | [[Category: Wei, H.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
[[Category: ghkl nucleotide-binding fold]] | [[Category: ghkl nucleotide-binding fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:02 2008'' |
Revision as of 22:43, 30 March 2008
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| , resolution 2.51Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | TOP2A, TOP2 (Homo sapiens) | ||||||
| Activity: | DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 | ||||||
| Related: | 1ZXM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Human DNA topoisomerase IIa ATPase/ADP
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.
About this Structure
1ZXN is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Mon Mar 31 01:43:02 2008
