1zxn

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[[Image:1zxn.gif|left|200px]]
 
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{{Structure
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==Human DNA topoisomerase IIa ATPase/ADP==
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|PDB= 1zxn |SIZE=350|CAPTION= <scene name='initialview01'>1zxn</scene>, resolution 2.51&Aring;
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<StructureSection load='1zxn' size='340' side='right'caption='[[1zxn]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-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>
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<table><tr><td colspan='2'>[[1zxn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXN FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
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|GENE= TOP2A, TOP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxn OCA], [https://pdbe.org/1zxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zxn RCSB], [https://www.ebi.ac.uk/pdbsum/1zxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxn ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1zxm|1ZXM]]
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</table>
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|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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/TOP2A_HUMAN TOP2A_HUMAN] Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.<ref>PMID:22323612</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zx/1zxn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zxn ConSurf].
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<div style="clear:both"></div>
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'''Human DNA topoisomerase IIa ATPase/ADP'''
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==See Also==
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*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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1ZXN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXN OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16100112 16100112]
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[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bechis, S K.]]
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[[Category: Bechis SK]]
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[[Category: Ruthenburg, A J.]]
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[[Category: Ruthenburg AJ]]
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[[Category: Verdine, G L.]]
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[[Category: Verdine GL]]
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[[Category: Wei, H.]]
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[[Category: Wei H]]
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[[Category: ghkl nucleotide-binding fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:02 2008''
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Current revision

Human DNA topoisomerase IIa ATPase/ADP

PDB ID 1zxn

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