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[[Image:1bjt.gif|left|200px]]


{{Structure
==TOPOISOMERASE II RESIDUES 409-1201==
|PDB= 1bjt |SIZE=350|CAPTION= <scene name='initialview01'>1bjt</scene>, resolution 2.5&Aring;
<StructureSection load='1bjt' size='340' side='right'caption='[[1bjt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1bjt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1BJT FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjt OCA], [https://pdbe.org/1bjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bjt RCSB], [https://www.ebi.ac.uk/pdbsum/1bjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjt ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://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].
<div style="clear:both"></div>


'''TOPOISOMERASE II RESIDUES 409-1201'''
==See Also==
 
*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1BJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJT OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10201398 10201398]
[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Berger JM]]
[[Category: Berger, J M.]]
[[Category: Bogden CE]]
[[Category: Bogden, C E.]]
[[Category: Fass D]]
[[Category: Fass, D.]]
[[Category: dna topology]]
[[Category: dna-binding]]
[[Category: quaternary change]]
[[Category: topoisomerase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:11:59 2008''

Latest revision as of 09:36, 7 February 2024

TOPOISOMERASE II RESIDUES 409-1201TOPOISOMERASE II RESIDUES 409-1201

Structural highlights

1bjt is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Liu Q, Wang JC. Identification of active site residues in the "GyrA" half of yeast DNA topoisomerase II. J Biol Chem. 1998 Aug 7;273(32):20252-60. PMID:9685374
  2. ↑ Schmidt BH, Osheroff N, Berger JM. Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity. Nat Struct Mol Biol. 2012 Nov;19(11):1147-54. doi: 10.1038/nsmb.2388. Epub 2012, Sep 30. PMID:23022727 doi:http://dx.doi.org/10.1038/nsmb.2388

1bjt, resolution 2.50Å

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