7pa5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Complex between the beta-lactamase CMY-2 with an inhibitory nanobody== | |
| + | <StructureSection load='7pa5' size='340' side='right'caption='[[7pa5]], [[Resolution|resolution]] 3.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7pa5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelidae Camelidae] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PA5 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]] 3.184Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7pa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pa5 OCA], [https://pdbe.org/7pa5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pa5 RCSB], [https://www.ebi.ac.uk/pdbsum/7pa5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pa5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q53TY8_ECOLX Q53TY8_ECOLX] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Three soluble single-domain fragments derived from the unique variable region of camelid heavy-chain antibodies (VHHs) against the CMY-2 beta-lactamase behaved as inhibitors. The structure of the complex VHH cAb(CMY-2)(254)/CMY-2 showed that the epitope is close to the active site and that the CDR3 of the VHH protrudes into the catalytic site. The beta-lactamase inhibition pattern followed a mixed profile with a predominant noncompetitive component. The three isolated VHHs recognized overlapping epitopes since they behaved as competitive binders. Our study identified a binding site that can be targeted by a new class of beta-lactamase inhibitors designed on the sequence of the paratope. Furthermore, the use of mono- or bivalent VHH and rabbit polyclonal anti-CMY-2 antibodies enables the development of the first generation of enzyme-linked immunosorbent assay (ELISA) for the detection of CMY-2 produced by CMY-2-expressing bacteria, irrespective of resistotype. | ||
| - | + | Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C beta-Lactamases.,Cawez F, Mercuri PS, Morales-Yanez FJ, Maalouf R, Vandevenne M, Kerff F, Guerin V, Mainil J, Thiry D, Saulmont M, Vanderplasschen A, Lafaye P, Ayme G, Bogaerts P, Dumoulin M, Galleni M Antimicrob Agents Chemother. 2023 Apr 18;67(4):e0149922. doi: , 10.1128/aac.01499-22. Epub 2023 Mar 9. PMID:36892280<ref>PMID:36892280</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7pa5" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Frederic | + | <references/> |
| - | [[Category: Frederic | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Camelidae]] | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Frederic Cawez FC]] | ||
| + | [[Category: Frederic Kerff FK]] | ||
| + | [[Category: Moreno Galleni MG]] | ||
| + | [[Category: Raphael Herman RH]] | ||
Current revision
Complex between the beta-lactamase CMY-2 with an inhibitory nanobody
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