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4bz3

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<StructureSection load='4bz3' size='340' side='right'caption='[[4bz3]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
<StructureSection load='4bz3' size='340' side='right'caption='[[4bz3]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bz3]] 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=4BZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZ3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bz3]] 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=4BZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZ3 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c09|4c09]], [[4c1c|4c1c]], [[4c1d|4c1d]], [[4c1e|4c1e]], [[4c1f|4c1f]], [[4c1g|4c1g]], [[4c1h|4c1h]]</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=4bz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bz3 OCA], [https://pdbe.org/4bz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bz3 RCSB], [https://www.ebi.ac.uk/pdbsum/4bz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bz3 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=4bz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bz3 OCA], [http://pdbe.org/4bz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bz3 RCSB], [http://www.ebi.ac.uk/pdbsum/4bz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bz3 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/Q9K2N0_PSEAI Q9K2N0_PSEAI]]
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beta-Lactams are the most successful antibacterials, but their effectiveness is threatened by resistance, most importantly by production of serine- and metallo-beta-lactamases (MBLs). MBLs are of increasing concern because they catalyse the hydrolysis of almost all beta-lactam antibiotics, including recent generation carbapenems. Clinically useful serine-beta-lactamase inhibitors have been developed, but such inhibitors are not available for MBLs. l-Captopril, used to treat hypertension via angiotensin-converting enzyme inhibition, has been reported to inhibit MBLs by chelating to the active site zinc ions via its thiol(ate). We report systematic studies on B1 MBL inhibition by all four captopril stereoisomers. High resolution crystal structures of three MBLs (IMP-1, BcII and VIM-2) in complex with either l-or d-captopril stereoisomers reveal correlations between the binding modes and inhibition potency. The results will be useful in the design of MBL inhibitors with the breadth of selectivity required for clinical application against carbapenem-resistant Enterobacteriaceae and other MBL mediated resistant infections.
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Structural basis of metallo-beta-lactamase inhibition by captopril stereoisomers.,Brem J, van Berkel SS, Zollman D, Lee SY, Gileadi O, McHugh PJ, Walsh TR, McDonough MA, Schofield CJ Antimicrob Agents Chemother. 2015 Oct 19. pii: AAC.01335-15. PMID:26482303<ref>PMID:26482303</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 4bz3" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[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: Beta-lactamase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Berkel, S S.van]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Brem, J]]
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[[Category: Brem J]]
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[[Category: McDonough, M A]]
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[[Category: McDonough MA]]
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[[Category: Schofield, C J]]
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[[Category: Schofield CJ]]
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[[Category: Zollman, D]]
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[[Category: Zollman D]]
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[[Category: Antibiotic resistance]]
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[[Category: Van Berkel SS]]
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[[Category: Hydrolase]]
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[[Category: Mbl]]
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Revision as of 17:16, 7 September 2022

Crystal structure of the metallo-beta-lactamase VIM-2

PDB ID 4bz3

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