1d3y: Difference between revisions
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<StructureSection load='1d3y' size='340' side='right'caption='[[1d3y]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1d3y' size='340' side='right'caption='[[1d3y]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1d3y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3Y OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1d3y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D3Y FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3y OCA], [https://pdbe.org/1d3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3y RCSB], [https://www.ebi.ac.uk/pdbsum/1d3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TOP6A_METJA TOP6A_METJA]] Relaxes both positive and negative superturns and exhibits a strong decatenase activity.<ref>PMID:10545127</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Topoisomerase|Topoisomerase]] | *[[Topoisomerase 3D structures|Topoisomerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:18, 10 March 2021
STRUCTURE OF THE DNA TOPOISOMERASE VI A SUBUNITSTRUCTURE OF THE DNA TOPOISOMERASE VI A SUBUNIT
Structural highlights
Function[TOP6A_METJA] Relaxes both positive and negative superturns and exhibits a strong decatenase activity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn all organisms, type II DNA topoisomerases are essential for untangling chromosomal DNA. We have determined the structure of the DNA-binding core of the Methanococcus jannaschii DNA topoisomerase VI A subunit at 2.0 A resolution. The overall structure of this subunit is unique, demonstrating that archaeal type II enzymes are distinct from other type II topoisomerases. However, the core structure contains a pair of domains that are also found in type IA and classic type II topoisomerases. Together, these regions may form the basis of a DNA cleavage mechanism shared among these enzymes. The core A subunit is a dimer that contains a deep groove that spans both protomers. The dimer architecture suggests that DNA is bound in the groove, across the A subunit interface, and that the two monomers separate during DNA transport. The A subunit of topoisomerase VI is homologous to the meiotic recombination factor, Spo11, and this structure can serve as a template for probing Spo11 function in eukaryotes. Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11.,Nichols MD, DeAngelis K, Keck JL, Berger JM EMBO J. 1999 Nov 1;18(21):6177-88. PMID:10545127[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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