4uwp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4uwp' size='340' side='right'caption='[[4uwp]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='4uwp' size='340' side='right'caption='[[4uwp]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uwp]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4uwp]] is a 1 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=4UWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UWP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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'>[https://proteopedia.org/fgij/fg.htm?mol=4uwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uwp OCA], [https://pdbe.org/4uwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uwp RCSB], [https://www.ebi.ac.uk/pdbsum/4uwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uwp ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E5BDC6_KLEPN E5BDC6_KLEPN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Klebsiella pneumoniae]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bjerga | [[Category: Bjerga GEK]] | ||
[[Category: Edvardsen | [[Category: Edvardsen KSW]] | ||
[[Category: Leiros | [[Category: Leiros H-KS]] | ||
[[Category: Samuelsen | [[Category: Samuelsen O]] | ||
Revision as of 10:48, 29 March 2023
Penta Zn1 coordination. Leu224 in VIM-26 from Klebsiella pneumoniae has implications for drug binding.Penta Zn1 coordination. Leu224 in VIM-26 from Klebsiella pneumoniae has implications for drug binding.
Structural highlights
FunctionPublication Abstract from PubMedDuring the last decades antimicrobial resistance has become a global health problem. Metallo-beta-lactamases (MBLs) which are broad-spectrum beta-lactamases that inactivate virtually all beta-lactams including carbapenems, are contributing to this health problem. In this study a novel MBL variant, termed VIM-26, identified in a Klebsiella pneumoniae isolate was studied. VIM-26 belongs to the Verona integron-encoded metallo-beta-lactamase (VIM) family of MBLs and is a His224Leu variant of the well-characterized VIM-1 variant. In this study, we report the kinetic parameters, minimum inhibitory concentrations and crystal structures of a recombinant VIM-26 protein, and compare them to previously published data on VIM-1, VIM-2 and VIM-7. The kinetic parameters and minimum inhibitory concentration determinations show that VIM-26, like VIM-7, has higher penicillinase activity but lower cephalosporinase activity than VIM-1 and VIM-2. The four determined VIM-26 crystal structures revealed mono- and di-zinc forms, where the Zn1 ion has distorted tetrahedral coordination geometry with an additional water molecule (W2) at a distance of 2.6-3.7 A, which could be important during catalysis. The R2 drug binding site in VIM-26 is more open compared to VIM-2 and VIM-7 and neutrally charged due to Leu224 and Ser228. Thus, the VIM-26 drug binding properties are different from the VIM-2 (Tyr224/Arg228) and VIM-7 (His224/Arg228) structures, indicating a role of these residues in the substrate specificity. Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-beta-lactamases.,Leiros HK, Edvardsen KS, Bjerga GE, Samuelsen O FEBS J. 2015 Jan 19. doi: 10.1111/febs.13200. PMID:25601024[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||