2q2e: Difference between revisions
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==Crystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazei== | ==Crystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazei== | ||
<StructureSection load='2q2e' size='340' side='right' caption='[[2q2e]], [[Resolution|resolution]] 4.00Å' scene=''> | <StructureSection load='2q2e' size='340' side='right'caption='[[2q2e]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2q2e]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2q2e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_2053 Dsm 2053]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q2E FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">top6A ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">top6A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2209 DSM 2053]), top6B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2209 DSM 2053])</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=2q2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q2e OCA], [https://pdbe.org/2q2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q2e RCSB], [https://www.ebi.ac.uk/pdbsum/2q2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q2e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TOP6A_METMA TOP6A_METMA]] Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity).[HAMAP-Rule:MF_00132] [[https://www.uniprot.org/uniprot/TOP6B_METMA TOP6B_METMA]] Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity).[HAMAP-Rule:MF_00322] | ||
== 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]] | ||
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Dsm 2053]] | [[Category: Dsm 2053]] | ||
[[Category: Large Structures]] | |||
[[Category: Benedetti, P]] | [[Category: Benedetti, P]] | ||
[[Category: Berger, J M]] | [[Category: Berger, J M]] | ||
Revision as of 11:05, 25 June 2021
Crystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazeiCrystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazei
Structural highlights
Function[TOP6A_METMA] Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity).[HAMAP-Rule:MF_00132] [TOP6B_METMA] Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity).[HAMAP-Rule:MF_00322] 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 PubMedType II topoisomerases help disentangle chromosomes to facilitate cell division. To advance understanding of the structure and dynamics of these essential enzymes, we have determined the crystal structure of an archaeal type IIB topoisomerase, topo VI, at 4.0-A resolution. The 220-kDa heterotetramer adopts a 'twin-gate' architecture, in which a pair of ATPase domains at one end of the enzyme is poised to coordinate DNA movements into the enzyme and through a set of DNA-cleaving domains at the other end. Small-angle X-ray scattering studies show that nucleotide binding elicits a major structural reorganization that is propagated to the enzyme's DNA-cleavage center, explaining how ATP is coupled to DNA capture and strand scission. These data afford important insights into the mechanisms of topo VI and related proteins, including type IIA topoisomerases and the Spo11 meiotic recombination endonuclease. Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI.,Corbett KD, Benedetti P, Berger JM Nat Struct Mol Biol. 2007 Jul;14(7):611-9. Epub 2007 Jul 1. PMID:17603498[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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