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| | ==Crystal structure of E. coli Gyrase B co-complexed with PROP-2-YN-1-YL {[5-(4-PIPERIDIN-1-YL-2-PYRIDIN-3-YL-1,3-THIAZOL-5-YL)-1H-PYRAZOL-3-YL]METHYL}CARBAMATE inhibitor== | | ==Crystal structure of E. coli Gyrase B co-complexed with PROP-2-YN-1-YL {[5-(4-PIPERIDIN-1-YL-2-PYRIDIN-3-YL-1,3-THIAZOL-5-YL)-1H-PYRAZOL-3-YL]METHYL}CARBAMATE inhibitor== |
| - | <StructureSection load='3g7e' size='340' side='right' caption='[[3g7e]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3g7e' size='340' side='right'caption='[[3g7e]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G7E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B46:PROP-2-YN-1-YL+{[5-(4-PIPERIDIN-1-YL-2-PYRIDIN-3-YL-1,3-THIAZOL-5-YL)-1H-PYRAZOL-3-YL]METHYL}CARBAMATE'>B46</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g75|3g75]], [[3g7b|3g7b]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B46:PROP-2-YN-1-YL+{[5-(4-PIPERIDIN-1-YL-2-PYRIDIN-3-YL-1,3-THIAZOL-5-YL)-1H-PYRAZOL-3-YL]METHYL}CARBAMATE'>B46</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs4634 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7e OCA], [https://pdbe.org/3g7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g7e RCSB], [https://www.ebi.ac.uk/pdbsum/3g7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7e ProSAT]</span></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>
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| - | <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=3g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7e OCA], [http://pdbe.org/3g7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g7e RCSB], [http://www.ebi.ac.uk/pdbsum/3g7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C3SLN3_ECOLX C3SLN3_ECOLX]] 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 (By similarity).[RuleBase:RU003363][HAMAP-Rule:MF_01898] | + | [https://www.uniprot.org/uniprot/C3SLN3_ECOLX C3SLN3_ECOLX] 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 (By similarity).[RuleBase:RU003363][HAMAP-Rule:MF_01898] |
| | == 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== |
| - | *[[Gyrase|Gyrase]] | + | *[[Gyrase 3D Structures|Gyrase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Charifson, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Wei, Y]] | + | [[Category: Charifson P]] |
| - | [[Category: Isomerase]] | + | [[Category: Wei Y]] |
| - | [[Category: Isomerase-isomerase inhibitor complex]]
| + | |
| Structural highlights
Function
C3SLN3_ECOLX 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 (By similarity).[RuleBase:RU003363][HAMAP-Rule:MF_01898]
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 PubMed
Bacterial DNA gyrase is an attractive target for the investigation of new antibacterial agents. Inhibitors of the GyrB subunit, which contains the ATP-binding site, are described in this communication. Novel, substituted 5-(1H-pyrazol-3-yl)thiazole compounds were identified as inhibitors of bacterial gyrase. Structure-guided optimization led to greater enzymatic potency and moderate antibacterial potency. Data are presented for the demonstration of selective enzyme inhibition of Escherichia coli GyrB over Staphylococcus aureus GyrB.
Discovery of pyrazolthiazoles as novel and potent inhibitors of bacterial gyrase.,Ronkin SM, Badia M, Bellon S, Grillot AL, Gross CH, Grossman TH, Mani N, Parsons JD, Stamos D, Trudeau M, Wei Y, Charifson PS Bioorg Med Chem Lett. 2010 May 1;20(9):2828-31. doi: 10.1016/j.bmcl.2010.03.052. , Epub 2010 Mar 15. PMID:20356737[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ronkin SM, Badia M, Bellon S, Grillot AL, Gross CH, Grossman TH, Mani N, Parsons JD, Stamos D, Trudeau M, Wei Y, Charifson PS. Discovery of pyrazolthiazoles as novel and potent inhibitors of bacterial gyrase. Bioorg Med Chem Lett. 2010 May 1;20(9):2828-31. doi: 10.1016/j.bmcl.2010.03.052. , Epub 2010 Mar 15. PMID:20356737 doi:10.1016/j.bmcl.2010.03.052
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