View source for 6enh


==Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with an aminocoumarin==
<StructureSection load='6enh' size='340' side='right'caption='[[6enh]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6enh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ENH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ENH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BHW:Coumermycin+A1'>BHW</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gyrB, TTHA1586 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=6enh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6enh OCA], [http://pdbe.org/6enh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6enh RCSB], [http://www.ebi.ac.uk/pdbsum/6enh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6enh ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GYRB_THET8 GYRB_THET8]] A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner (PubMed:23804759, PubMed:11850422). It probably also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes (PubMed:11850422). Relaxes negatively supercoiled DNA in an ATP-independent manner (PubMed:23804759, PubMed:11850422). At comparable concentrations T.thermophilus gyrase does not introduce as many negative supercoils into DNA as the E.coli enzyme (PubMed:23804759).<ref>PMID:23804759</ref>   Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. 
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== Publication Abstract from PubMed ==
Coumermycin A1 is a natural aminocoumarin that inhibits bacterial DNA gyrase, a member of the GHKL proteins superfamily. We report here the first cocrystal structures of gyrase B bound to coumermycin A1, revealing that one coumermycin A1 molecule traps simultaneously two ATP-binding sites. The inhibited dimers from different species adopt distinct sequence-dependent conformations, alternative to the ATP-bound form. These structures provide a basis for the rational development of coumermycin A1 derivatives for antibiotherapy and biotechnology applications.

Structural Basis for DNA Gyrase Interaction with Coumermycin A1.,Vanden Broeck A, McEwen AG, Chebaro Y, Potier N, Lamour V J Med Chem. 2019 Apr 3. doi: 10.1021/acs.jmedchem.8b01928. PMID:30920824<ref>PMID:30920824</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 6enh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thet8]]
[[Category: Broeck, A Vanden]]
[[Category: Lamour, V]]
[[Category: McEwen, A G]]
[[Category: Gyrase b-aminocoumarin complex]]
[[Category: Isomerase]]
[[Category: Topoisomerase]]