View source for 7uon


==CTX-M-14 Y105W mutant==
<StructureSection load='7uon' size='340' side='right'caption='[[7uon]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7uon]] is a 1 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=7UON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UON 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]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7uon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uon OCA], [https://pdbe.org/7uon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uon RCSB], [https://www.ebi.ac.uk/pdbsum/7uon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uon ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H6UQI0_ECOLX H6UQI0_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CTX-M beta-lactamases are prevalent antibiotic resistance enzymes and are notable for their ability to rapidly hydrolyze the extended-spectrum cephalosporin, cefotaxime. We hypothesized that the active site sequence requirements of CTX-M-mediated hydrolysis differ between classes of beta-lactam antibiotics. Accordingly, we use codon randomization, antibiotic selection, and deep sequencing to determine the CTX-M active-site residues required for hydrolysis of cefotaxime and the penicillin, ampicillin. The study reveals positions required for hydrolysis of all beta-lactams, as well as residues controlling substrate specificity. Further, CTX-M enzymes poorly hydrolyze the extended-spectrum cephalosporin, ceftazidime. We further show that the sequence requirements for ceftazidime hydrolysis follow those of cefotaxime, with the exception that key active-site omega loop residues are not required, and may be detrimental, for ceftazidime hydrolysis. These results provide insights into cephalosporin hydrolysis and demonstrate that changes to the active-site omega loop are likely required for the evolution of CTX-M-mediated ceftazidime resistance.

Mapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M beta-lactamase.,Judge A, Hu L, Sankaran B, Van Riper J, Venkataram Prasad BV, Palzkill T Commun Biol. 2023 Jan 12;6(1):35. doi: 10.1038/s42003-023-04422-z. PMID:36635385<ref>PMID:36635385</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7uon" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Hu L]]
[[Category: Judge A]]
[[Category: Palzkill T]]
[[Category: Prasad BVV]]
[[Category: Sankaran B]]
[[Category: Van Riper J]]