View source for 6nvt


==Crystal structure of TLA-1 extended spectrum Beta-lactamase==
<StructureSection load='6nvt' size='340' side='right'caption='[[6nvt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X6W1_ECOLX Q9X6W1_ECOLX] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nvt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Cifuentes-Castro VH]]
[[Category: Rodriguez-Almazan C]]
[[Category: Rudino-Pinera E]]