View source for 9raj


==Class A CTX-M-14 E166A mutant in complex with Dicloxacillin at room temperature==
<StructureSection load='9raj' size='340' side='right'caption='[[9raj]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9raj]] 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=9RAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RAJ 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DXU:(3R,4R,5R)-3-(2,6-DICHLOROPHENYL)-N-{(1R)-1-[(2R,4S)-4-(DIHYDROXYMETHYL)-5,5-DIMETHYL-1,3-THIAZOLIDIN-2-YL]-2-OXOETHYL}-5-METHYL-1,2-OXAZOLIDINE-4-CARBOXAMIDE'>DXU</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=9raj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9raj OCA], [https://pdbe.org/9raj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9raj RCSB], [https://www.ebi.ac.uk/pdbsum/9raj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9raj 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9raj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Gore G]]
[[Category: Schulz EC]]