View source for 1bjt


==TOPOISOMERASE II RESIDUES 409-1201==
<StructureSection load='1bjt' size='340' side='right'caption='[[1bjt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BJT FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjt OCA], [http://pdbe.org/1bjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bjt RCSB], [http://www.ebi.ac.uk/pdbsum/1bjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjt ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TOP2_YEAST TOP2_YEAST]] 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:9685374</ref> <ref>PMID:23022727</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/1bjt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1bjt ConSurf].
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== Publication Abstract from PubMed ==
Type II DNA topoisomerases mediate the passage of one DNA duplex through a transient break in another, an event essential for chromosome segregation and cell viability. The active sites of the type II topoisomerase dimer associate covalently with the DNA break-points and must separate by at least the width of the second DNA duplex to accommodate transport. A new structure of the Saccharomyces cerevisiae topoisomerase II DNA-binding and cleavage core suggests that in addition to conformational changes in the DNA-opening platform, a dramatic reorganization of accessory domains may occur during catalysis. These conformational differences have implications for both the DNA-breaking and duplex-transport events in the topo II reaction mechanism, suggest a mechanism by which two distinct drug-resistance loci interact, and illustrate the scope of structural changes in the cycling of molecular machines.

Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands.,Fass D, Bogden CE, Berger JM Nat Struct Biol. 1999 Apr;6(4):322-6. PMID:10201398<ref>PMID:10201398</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1bjt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Topoisomerase|Topoisomerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Berger, J M]]
[[Category: Bogden, C E]]
[[Category: Fass, D]]
[[Category: Dna topology]]
[[Category: Dna-binding]]
[[Category: Quaternary change]]
[[Category: Topoisomerase]]