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| | <StructureSection load='2y91' size='340' side='right'caption='[[2y91]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2y91' size='340' side='right'caption='[[2y91]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y91]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y91 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Y91 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y91]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y91 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=98J:5-HYDROXY-3-OXOPENTANOIC+ACID'>98J</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1X6:O-[(2E)-3-AMINOPROP-2-ENOYL]-L-SERINE'>1X6</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1X6:O-[(2E)-3-AMINOPROP-2-ENOYL]-L-SERINE'>1X6</scene>, <scene name='pdbligand=98J:5-HYDROXY-3-OXOPENTANOIC+ACID'>98J</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x71|2x71]]</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=2y91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y91 OCA], [https://pdbe.org/2y91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y91 RCSB], [https://www.ebi.ac.uk/pdbsum/2y91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y91 ProSAT]</span></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'>[http://proteopedia.org/fgij/fg.htm?mol=2y91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y91 OCA], [http://pdbe.org/2y91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y91 RCSB], [http://www.ebi.ac.uk/pdbsum/2y91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y91 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BLAC_BACLI BLAC_BACLI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus licheniformis]] | | [[Category: Bacillus licheniformis]] |
| - | [[Category: Beta-lactamase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Charlier, P]] | + | [[Category: Charlier P]] |
| - | [[Category: Herman, R]] | + | [[Category: Herman R]] |
| - | [[Category: Kerff, F]] | + | [[Category: Kerff F]] |
| - | [[Category: Power, P]] | + | [[Category: Power P]] |
| - | [[Category: Sauvage, E]] | + | [[Category: Sauvage E]] |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
BLAC_BACLI
Publication Abstract from PubMed
OBJECTIVES: Our aim was to unravel the inactivation pathway of the class A beta-lactamase produced by Bacillus licheniformis BS3 (BS3) by clavulanate. METHODS: The interaction between clavulanate and BS3 was studied by X-ray crystallography, pre-steady-state kinetics and mass spectrometry. RESULTS: The analysis of the X-ray structure of the complex yielded by the reaction between clavulanate and BS3 indicates that the transient inactivated form, namely the cis-trans enamine complex, is hydrolysed to an ethane-imine ester covalently linked to the active site serine and a pentan-3-one-5-ol acid. It is the first time that this mechanism has been observed in an inactivated beta-lactamase. Furthermore, the ionic interactions made by the carboxylic group of pentan-3-one-5-ol may provide an understanding of the decarboxylation process of the trans-enamine observed in the non-productive complex observed for the interaction between clavulanate and SHV-1 and Mycobacterium tuberculosis beta-lactamase (Mtu). CONCLUSIONS: This work provides a comprehensive clavulanate hydrolysis pathway accounting for the observed acyl-enzyme structures of class A beta-lactamase/clavulanate adducts.
Novel fragments of clavulanate observed in the structure of the class A beta-lactamase from Bacillus licheniformis BS3.,Power P, Mercuri P, Herman R, Kerff F, Gutkind G, Dive G, Galleni M, Charlier P, Sauvage E J Antimicrob Chemother. 2012 Oct;67(10):2379-87. Epub 2012 Jul 6. PMID:22773738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Power P, Mercuri P, Herman R, Kerff F, Gutkind G, Dive G, Galleni M, Charlier P, Sauvage E. Novel fragments of clavulanate observed in the structure of the class A beta-lactamase from Bacillus licheniformis BS3. J Antimicrob Chemother. 2012 Oct;67(10):2379-87. Epub 2012 Jul 6. PMID:22773738 doi:http://dx.doi.org/10.1093/jac/dks231
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