6nvt
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of TLA-1 extended spectrum Beta-lactamase== | |
| + | <StructureSection load='6nvt' size='340' side='right'caption='[[6nvt]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6nvt]] is a 4 chain structure. 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> | ||
| + | </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> | ||
| + | <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=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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:31780261</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6nvt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-lactamase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cifuentes-Castro, V H]] | ||
| + | [[Category: Rodriguez-Almazan, C]] | ||
| + | [[Category: Rudino-Pinera, E]] | ||
| + | [[Category: Antibiotic]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Lactamase]] | ||
| + | [[Category: Resistance]] | ||
Revision as of 15:08, 11 December 2019
Crystal structure of TLA-1 extended spectrum Beta-lactamase
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