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| | <StructureSection load='2whg' size='340' side='right'caption='[[2whg]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2whg' size='340' side='right'caption='[[2whg]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2whg]] 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=2WHG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WHG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2whg]] 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=2WHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WHG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9Å</td></tr> |
| - | <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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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'>[http://proteopedia.org/fgij/fg.htm?mol=2whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whg OCA], [http://pdbe.org/2whg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2whg RCSB], [http://www.ebi.ac.uk/pdbsum/2whg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2whg ProSAT]</span></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=2whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whg OCA], [https://pdbe.org/2whg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2whg RCSB], [https://www.ebi.ac.uk/pdbsum/2whg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2whg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8KRJ3_PSEAI Q8KRJ3_PSEAI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ferrer, J L]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Galleni, M]] | + | [[Category: Ferrer JL]] |
| - | [[Category: Lassaux, P]] | + | [[Category: Galleni M]] |
| - | [[Category: Traore, D A.K]] | + | [[Category: Lassaux P]] |
| - | [[Category: Alpha-beta/beta-alpha fold]] | + | [[Category: Traore DAK]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q8KRJ3_PSEAI
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
The metallo-beta-lactamase VIM-4, mainly found in Pseudomonas aeruginosa or Acinetobacter baumannii was produced in Escherichia coli and characterized by biochemical and X-ray techniques. A detailed kinetic study performed in the presence of Zn(2+) concentration ranging from 0.4 to 100 muM showed that VIM-4 exhibits a kinetic profile similar to those of VIM-2 and VIM-1. However, VIM-4 is more active than VIM-1 against benzylpenicillin, cephalothin, nitrocefin and imipenem and less active than VIM-2 against ampicillin and meropenem. The crystal structure of the di-zinc form of VIM-4 was solved at 1.9 A. The sole difference between VIM-4 and VIM-1 is found at residue 228 which is Ser in VIM-1 and Arg in VIM-4. This substitution has a major impact on the VIM-4 catalytic efficiency when compared to VIM-1. By contrast, the differences between VIM-2 and VIM-4 seem due to a different position of the "flapping loop" and two substitutions in loop 2. Study of the thermal stability and the activity of the holo- and apo-VIM-4 enzymes revealed that Zn(2+) ions have a pronounced stabilizing effect on the enzyme and are necessary for preserving the structure.
Biochemical and Structural Characterization of the Subclass B1 Metallo-{beta}-Lactamase VIM-4.,Lassaux P, Traore DA, Loisel E, Favier A, Docquier JD, Sohier JS, Laurent C, Bebrone C, Frere JM, Ferrer JL, Galleni M Antimicrob Agents Chemother. 2010 Dec 13. PMID:21149620[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lassaux P, Traore DA, Loisel E, Favier A, Docquier JD, Sohier JS, Laurent C, Bebrone C, Frere JM, Ferrer JL, Galleni M. Biochemical and Structural Characterization of the Subclass B1 Metallo-{beta}-Lactamase VIM-4. Antimicrob Agents Chemother. 2010 Dec 13. PMID:21149620 doi:10.1128/AAC.01486-09
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