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5k48

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==VIM-2 Metallo Beta Lactamase in complex with 3-(mercaptomethyl)-[1,1'-biphenyl]-4-carboxylic acid==
==VIM-2 Metallo Beta Lactamase in complex with 3-(mercaptomethyl)-[1,1'-biphenyl]-4-carboxylic acid==
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<StructureSection load='5k48' size='340' side='right' caption='[[5k48]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
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<StructureSection load='5k48' size='340' side='right'caption='[[5k48]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5k48]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K48 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5k48]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K48 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=S5Z:4-phenyl-2-(sulfanylmethyl)benzoic+acid'>S5Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.744&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaVIM-2, bla vim-2, bla-VIM-2, blasVIM-2, blaVIM2, blm, VIM-2, vim-2, PAERUG_P32_London_17_VIM_2_10_11_06255 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=S5Z:4-phenyl-2-(sulfanylmethyl)benzoic+acid'>S5Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5k48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k48 OCA], [http://pdbe.org/5k48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k48 RCSB], [http://www.ebi.ac.uk/pdbsum/5k48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k48 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k48 OCA], [https://pdbe.org/5k48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k48 RCSB], [https://www.ebi.ac.uk/pdbsum/5k48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k48 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9K2N0_PSEAI Q9K2N0_PSEAI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Zinc ion-dependent beta-lactamases (MBLs) catalyze the hydrolysis of almost all beta-lactam antibiotics and resist the action of clinically available beta-lactamase inhibitors. We report how application of in silico fragment-based molecular design employing thiol-mediated metal anchorage leads to potent MBL inhibitors. The new inhibitors manifest potent inhibition of clinically important B1 subfamily MBLs, including the widespread NDM-1, IMP-1, and VIM-2 enzymes; with lower potency, some of them also inhibit clinically relevant Class A and D serine-beta-lactamases. The inhibitors show selectivity for bacterial MBL enzymes compared to that for human MBL fold nucleases. Cocrystallization of one inhibitor, which shows potentiation of Meropenem activity against MBL-expressing Enterobacteriaceae, with VIM-2 reveals an unexpected binding mode, involving interactions with residues from conserved active site bordering loops.
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In Silico Fragment-Based Design Identifies Subfamily B1 Metallo-beta-lactamase Inhibitors.,Cain R, Brem J, Zollman D, McDonough MA, Johnson RM, Spencer J, Makena A, Abboud MI, Cahill S, Lee SY, McHugh PJ, Schofield CJ, Fishwick CWG J Med Chem. 2018 Jan 10. doi: 10.1021/acs.jmedchem.7b01728. PMID:29271657<ref>PMID:29271657</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5k48" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Brem, J]]
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[[Category: Large Structures]]
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[[Category: McDonough, M]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Schofield, C]]
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[[Category: Brem J]]
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[[Category: Zollman, D]]
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[[Category: McDonough M]]
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[[Category: Antibiotic resistance]]
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[[Category: Schofield C]]
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[[Category: Carbapenamase. inhibitor]]
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[[Category: Zollman D]]
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[[Category: Hydrolase]]
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[[Category: Metallo beta-lactamase]]
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Current revision

VIM-2 Metallo Beta Lactamase in complex with 3-(mercaptomethyl)-[1,1'-biphenyl]-4-carboxylic acid

PDB ID 5k48

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