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9rao
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Class A CTX-M-14 E166A mutant in complex with Cloxacillin at room temperature== | |
| + | <StructureSection load='9rao' size='340' side='right'caption='[[9rao]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9rao]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RAO 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]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXU:CLOXACILLIN+(OPEN+FORM)'>CXU</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=9rao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rao OCA], [https://pdbe.org/9rao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rao RCSB], [https://www.ebi.ac.uk/pdbsum/9rao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rao ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0H3H219_KLEPH A0A0H3H219_KLEPH] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The predominant resistance mechanism observed in Gram-negative bacteria involves the production of beta-lactamases, which catalyse the hydrolysis of beta-lactam antibiotics, thereby rendering them ineffective. Although Isoxazolyl Penicillins have been available since the 1970s, there are currently no structures in complex with class-A beta-lactamases available. Here we have analysed the structure of the clinically relevant beta-lactamase CTX-M-14 from Klebsiella pneumoniae near physiological temperatures, via serial synchrotron crystallography. We demonstrate the acyl-enzyme intermediates of the catalytically impaired CTX-M-14 mutant E166A in complex with three Isoxazolyl-Penicillins: Oxacillin, Cloxacillin and Dicloxacillin. Structural comparisons of CTX-M-Penicillin complexes show that, while conserved active-site interactions are maintained, each Isoxazolyl-Penicillin adopts a distinct conformation. While the three derivatives differ only by one and two chlorine atoms, respectively, their conformational heterogeneity appears to be increased by chlorination of the phenyl ring. | ||
| - | + | Binding mode of Isoxazolyl Penicillins to a Class-A beta-lactamase at ambient conditions.,Gore G, Prester A, von Stetten D, Bartels K, Schulz EC Commun Chem. 2025 Dec 1;8(1):387. doi: 10.1038/s42004-025-01801-x. PMID:41326695<ref>PMID:41326695</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9rao" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Klebsiella pneumoniae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gore G]] | ||
| + | [[Category: Schulz EC]] | ||
Current revision
Class A CTX-M-14 E166A mutant in complex with Cloxacillin at room temperature
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