6eng: Difference between revisions

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-'''Unreleased structure'''
-The entry 6eng is ON HOLD
+==Crystal structure of the 43K ATPase domain of Escherichia coli gyrase B in complex with an aminocoumarin==
+<StructureSection load='6eng' size='340' side='right'caption='[[6eng]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6eng]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ENG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ENG 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6eng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eng OCA], [http://pdbe.org/6eng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eng RCSB], [http://www.ebi.ac.uk/pdbsum/6eng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eng ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GYRB_ECOLI GYRB_ECOLI]] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings.<ref>PMID:12051843</ref> <ref>PMID:18642932</ref> <ref>PMID:20675723</ref>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Vanden Broeck, A., McEwen, A.G., Lamour, V.
+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>
-Description: Crystal structure of the 43K ATPase domain of Escherichia coli gyrase B in complex with an aminocoumarin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Vanden Broeck, A]]
+<div class="pdbe-citations 6eng" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Broeck, A Vanden]]
 [[Category: Lamour, V]]
-[[Category: Mcewen, A.G]]
+[[Category: McEwen, A G]]
+[[Category: Gyrase b-aminocoumarin complex]]
+[[Category: Isomerase]]
+[[Category: Topoisomerase]]