5a87: Difference between revisions
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<StructureSection load='5a87' size='340' side='right'caption='[[5a87]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='5a87' size='340' side='right'caption='[[5a87]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a87]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5a87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A87 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a87 OCA], [https://pdbe.org/5a87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a87 RCSB], [https://www.ebi.ac.uk/pdbsum/5a87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a87 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8GKX2_KLEPN Q8GKX2_KLEPN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Brem | [[Category: Brem J]] | ||
[[Category: Duzgun | [[Category: Duzgun AO]] | ||
[[Category: McDonough | [[Category: McDonough MA]] | ||
[[Category: Schofield | [[Category: Schofield CJ]] | ||
Latest revision as of 14:05, 10 January 2024
Crystal structure of the metallo-beta-lactamase VIM-5Crystal structure of the metallo-beta-lactamase VIM-5
Structural highlights
FunctionPublication Abstract from PubMedMetallo-beta-lactamases (MBLs) are of increasing clinical significance; the development of clinically useful MBL inhibitors is challenged by the rapid evolution of variant MBLs. The Verona integron-borne metallo-beta-lactamase (VIM) enzymes are among the most widely distributed MBLs, with >40 VIM variants having been reported. We report on the crystallographic analysis of VIM-5 and comparison of biochemical and biophysical properties of VIM-1, VIM-2, VIM-4, VIM-5, and VIM-38. Recombinant VIM variants were produced and purified, and their secondary structure and thermal stabilities were investigated by circular dichroism analyses. Steady-state kinetic analyses with a representative panel of beta-lactam substrates were carried out to compare the catalytic efficiencies of the VIM variants. Furthermore, a set of metalloenzyme inhibitors were screened to compare their effects on the different VIM variants. The results reveal only small variations in the kinetic parameters of the VIM variants but substantial differences in their thermal stabilities and inhibition profiles. Overall, these results support the proposal that protein stability may be a factor in MBL evolution and highlight the importance of screening MBL variants during inhibitor development programs. Comparison of Verona Integron-Borne Metallo-beta-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition Profiles.,Makena A, Duzgun AO, Brem J, McDonough MA, Rydzik AM, Abboud MI, Saral A, Cicek AC, Sandalli C, Schofield CJ Antimicrob Agents Chemother. 2015 Dec 14;60(3):1377-84. doi:, 10.1128/AAC.01768-15. PMID:26666919[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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