1mu5

<table><tr><td colspan='2'>[[1mu5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51178 Atcc 51178]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MU5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mx0|1mx0]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">top6b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2286 ATCC 51178])</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://proteopedia.org/fgij/fg.htm?mol=1mu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu5 OCA], [http://pdbe.org/1mu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mu5 RCSB], [http://www.ebi.ac.uk/pdbsum/1mu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mu5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TOP6B_SULSH TOP6B_SULSH]] Relaxes both positive and negative superturns and exhibits a strong decatenase activity.[HAMAP-Rule:MF_00322]

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== Publication Abstract from PubMed ==

Type IIA and type IIB topoisomerases each possess the ability to pass one DNA duplex through another in an ATP-dependent manner. The role of ATP in the strand passage reaction is poorly understood, particularly for the type IIB (topoisomerase VI) family. We have solved the structure of the ATP-binding subunit of topoisomerase VI (topoVI-B) in two states: an unliganded monomer and a nucleotide-bound dimer. We find that topoVI-B is highly structurally homologous to the entire 40-43 kDa ATPase region of type IIA topoisomerases and MutL proteins. Nucleotide binding to topoVI-B leads to dimerization of the protein and causes dramatic conformational changes within each protomer. Our data demonstrate that type IIA and type IIB topoisomerases have descended from a common ancestor and reveal how ATP turnover generates structural signals in the reactions of both type II topoisomerase families. When combined with the structure of the A subunit to create a picture of the intact topoisomerase VI holoenzyme, the ATP-driven motions of topoVI-B reveal a simple mechanism for strand passage by the type IIB topoisomerases.

Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution.,Corbett KD, Berger JM EMBO J. 2003 Jan 2;22(1):151-63. PMID:12505993<ref>PMID:12505993</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 1mu5" style="background-color:#fffaf0;"></div>

[[Category: Atcc 51178]]

[[Category: Berger, J M]]

[[Category: Corbett, K D]]

[[Category: Ghkl atpase]]

[[Category: Isomerase]]