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| | <StructureSection load='6nvt' size='340' side='right'caption='[[6nvt]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6nvt' size='340' side='right'caption='[[6nvt]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6nvt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NVT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nvt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NVT 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tla-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6nvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nvt OCA], [https://pdbe.org/6nvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nvt RCSB], [https://www.ebi.ac.uk/pdbsum/6nvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nvt ProSAT]</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=6nvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nvt OCA], [http://pdbe.org/6nvt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nvt RCSB], [http://www.ebi.ac.uk/pdbsum/6nvt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nvt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9X6W1_ECOLX Q9X6W1_ECOLX] |
| | <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 6nvt" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6nvt" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cifuentes-Castro, V H]] | + | [[Category: Cifuentes-Castro VH]] |
| - | [[Category: Rodriguez-Almazan, C]] | + | [[Category: Rodriguez-Almazan C]] |
| - | [[Category: Rudino-Pinera, E]] | + | [[Category: Rudino-Pinera E]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lactamase]]
| + | |
| - | [[Category: Resistance]]
| + | |
| Structural highlights
Function
Q9X6W1_ECOLX
Publication Abstract from PubMed
beta-lactamases are the main molecules responsible for giving bacterial resistance against beta-lactam antibiotics. The study of beta-lactamases has allowed the development of antibiotics capable of inhibiting these enzymes. In this context, extended spectrum beta-lactamase (ESBL) TLA-1 has spread in Escherichia coli and Enterobacter cloacae clinical isolates during the last 30 years in Mexico. In this research, the 3D structures of ESBL TLA-1 and TLA-1 S70G mutant, both ligand-free and in complex with clavulanic acid were determined by X-ray crystallography. Four clavulanic acid molecules were found in the structure of TLA-1, two of those were intermediaries of the acylation process and were localized covalently bound to two different amino acid residues, Ser70 and Ser237. The coordinates of TLA-1 in complex with clavulanic acid shows the existence of a second acylation site, additional to Ser70, which might be extendable to several members of the subclass A beta-lactamases family. This is the first time that two serines involved in binding clavulanic acid has been reported and described to an atomic level.
The crystal structure of ESBL TLA-1 in complex with clavulanic acid reveals a second acylation site.,Cifuentes-Castro V, Rodriguez-Almazan C, Silva-Sanchez J, Rudino-Pinera E Biochem Biophys Res Commun. 2019 Nov 25. pii: S0006-291X(19)32266-1. doi:, 10.1016/j.bbrc.2019.11.138. PMID:31780261[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cifuentes-Castro V, Rodriguez-Almazan C, Silva-Sanchez J, Rudino-Pinera E. The crystal structure of ESBL TLA-1 in complex with clavulanic acid reveals a second acylation site. Biochem Biophys Res Commun. 2019 Nov 25. pii: S0006-291X(19)32266-1. doi:, 10.1016/j.bbrc.2019.11.138. PMID:31780261 doi:http://dx.doi.org/10.1016/j.bbrc.2019.11.138
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