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| | <StructureSection load='2uyx' size='340' side='right'caption='[[2uyx]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='2uyx' size='340' side='right'caption='[[2uyx]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2uyx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2UYX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2uyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UYX FirstGlance]. <br> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bc2|1bc2]], [[1bmc|1bmc]], [[1bvt|1bvt]], [[1dxk|1dxk]], [[1mqo|1mqo]], [[2bc2|2bc2]], [[2bfk|2bfk]], [[2bfl|2bfl]], [[2bfz|2bfz]], [[2bg2|2bg2]], [[2bg6|2bg6]], [[2bg7|2bg7]], [[2bg8|2bg8]], [[2bga|2bga]], [[3bc2|3bc2]]</td></tr> | + | <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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2uyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyx OCA], [https://pdbe.org/2uyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uyx RCSB], [https://www.ebi.ac.uk/pdbsum/2uyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyx ProSAT]</span></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=2uyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyx OCA], [http://pdbe.org/2uyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uyx RCSB], [http://www.ebi.ac.uk/pdbsum/2uyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE]] Can hydrolyze carbapenem compounds. | + | [https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds. |
| | == 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: Atcc 14579]] | + | [[Category: Bacillus cereus]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bennett, B]] | + | [[Category: Bennett B]] |
| - | [[Category: Fabiane, S M]] | + | [[Category: Fabiane SM]] |
| - | [[Category: Kowalski, J M]] | + | [[Category: Kowalski JM]] |
| - | [[Category: Larrull, L I]] | + | [[Category: Larrull LI]] |
| - | [[Category: Sutton, B J]] | + | [[Category: Sutton BJ]] |
| - | [[Category: Vila, A J]] | + | [[Category: Vila AJ]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Metallo beta- lactamase]]
| + | |
| - | [[Category: Penicillinase]]
| + | |
| Structural highlights
Function
BLA2_BACCE Can hydrolyze carbapenem compounds.
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
Metallo-beta-lactamases are zinc-dependent hydrolases that inactivate beta-lactam antibiotics, rendering bacteria resistant to them. Asp-120 is fully conserved in all metallo-beta-lactamases and is central to catalysis. Several roles have been proposed for Asp-120, but so far there is no agreed consensus. We generated four site-specifically substituted variants of the enzyme BcII from Bacillus cereus as follows: D120N, D120E, D120Q, and D120S. Replacement of Asp-120 by other residues with very different metal ligating capabilities severely impairs the lactamase activity without abolishing metal binding to the mutated site. A kinetic study of these mutants indicates that Asp-120 is not the proton donor, nor does it play an essential role in nucleophilic activation. Spectroscopic and crystallographic analysis of D120S BcII, the least active mutant bearing the weakest metal ligand in the series, reveals that this enzyme is able to accommodate a dinuclear center and that perturbations in the active site are limited to the Zn2 site. It is proposed that the role of Asp-120 is to act as a strong Zn2 ligand, locating this ion optimally for substrate binding, stabilization of the development of a partial negative charge in the beta-lactam nitrogen, and protonation of this atom by a zinc-bound water molecule.
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity.,Llarrull LI, Fabiane SM, Kowalski JM, Bennett B, Sutton BJ, Vila AJ J Biol Chem. 2007 Jun 22;282(25):18276-85. Epub 2007 Apr 10. PMID:17426028[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Llarrull LI, Fabiane SM, Kowalski JM, Bennett B, Sutton BJ, Vila AJ. Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity. J Biol Chem. 2007 Jun 22;282(25):18276-85. Epub 2007 Apr 10. PMID:17426028 doi:10.1074/jbc.M700742200
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