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| | ==Crystal structure of BlaC from Mycobacterium tuberculosis== | | ==Crystal structure of BlaC from Mycobacterium tuberculosis== |
| - | <StructureSection load='5oyo' size='340' side='right' caption='[[5oyo]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5oyo' size='340' side='right'caption='[[5oyo]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oyo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OYO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oyo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OYO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nj2|5nj2]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaC, ERS027646_02769 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=5oyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oyo OCA], [https://pdbe.org/5oyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oyo RCSB], [https://www.ebi.ac.uk/pdbsum/5oyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oyo 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5oyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oyo OCA], [http://pdbe.org/5oyo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oyo RCSB], [http://www.ebi.ac.uk/pdbsum/5oyo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oyo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BLAC_MYCTU BLAC_MYCTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5oyo" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5oyo" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pannu, N S]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Tassoni, R]] | + | [[Category: Pannu NS]] |
| - | [[Category: Hydrolase]] | + | [[Category: Tassoni R]] |
| Structural highlights
Function
BLAC_MYCTU
Publication Abstract from PubMed
The rise of multi- and even totally antibiotic resistant forms of Mycobacterium tuberculosis underlines the need for new antibiotics. The pathogen is resistant to beta-lactam compounds due to its native serine beta-lactamase, BlaC. This resistance can be circumvented by administration of a beta-lactamase inhibitor. We studied the interaction between BlaC and the inhibitor clavulanic acid. Our data show hydrolysis of clavulanic acid and recovery of BlaC activity upon prolonged incubation. The rate of clavulanic acid hydrolysis is much higher in the presence of phosphate ions. A specific binding site for phosphate is identified in the active site pocket, both in the crystalline state and in solution. NMR spectroscopy experiments show that phosphate binds to this site with a dissociation constant of 30 mM in the free enzyme. We conclude that inhibition of BlaC by clavulanic acid is reversible and that phosphate ions can promote the hydrolysis of the inhibitor.
Phosphate Promotes the Recovery of Mycobacterium tuberculosis beta-Lactamase from Clavulanic Acid Inhibition.,Elings W, Tassoni R, van der Schoot SA, Luu W, Kynast JP, Dai L, Blok AJ, Timmer M, Florea BI, Pannu NS, Ubbink M Biochemistry. 2017 Nov 14. doi: 10.1021/acs.biochem.7b00556. PMID:29087696[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Elings W, Tassoni R, van der Schoot SA, Luu W, Kynast JP, Dai L, Blok AJ, Timmer M, Florea BI, Pannu NS, Ubbink M. Phosphate Promotes the Recovery of Mycobacterium tuberculosis beta-Lactamase from Clavulanic Acid Inhibition. Biochemistry. 2017 Nov 14. doi: 10.1021/acs.biochem.7b00556. PMID:29087696 doi:http://dx.doi.org/10.1021/acs.biochem.7b00556
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