7n1m: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7n1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1M FirstGlance]. <br> | <table><tr><td colspan='2'>[[7n1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7n1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1m OCA], [https://pdbe.org/7n1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1m RCSB], [https://www.ebi.ac.uk/pdbsum/7n1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1m ProSAT]</span></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=7n1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1m OCA], [https://pdbe.org/7n1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1m RCSB], [https://www.ebi.ac.uk/pdbsum/7n1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BLO11_PSEAI BLO11_PSEAI] Hydrolyzes carbenicillin, oxacillin and cephalosporin. Does not hydrolyze cefoxitin or carbapenems. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic beta-lactamase AmpC. However, OXA-10-family beta-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA beta-lactamases have a propensity for mutation that leads to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk P. aeruginosa clonal complex CC446 with a resistance to ceftazidime. A genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of bla(OXA-10), named bla(OXA-935), which was predicted to produce an OXA-10 variant with two amino acid substitutions: an aspartic acid instead of a glycine at position 157 and a serine instead of a phenylalanine at position 153. The G157D mutation, present in OXA-14, is associated with the resistance of P. aeruginosa to ceftazidime. Compared to OXA-14, OXA-935 showed increased catalytic efficiency for ceftazidime. The deletion of bla(OXA-935) restored the sensitivity to ceftazidime, and susceptibility profiling of P. aeruginosa laboratory strains expressing bla(OXA-935) revealed that OXA-935 conferred ceftazidime resistance. To better understand the impacts of the variant amino acids, we determined the crystal structures of OXA-14 and OXA-935. Compared to OXA-14, the F153S mutation in OXA-935 conferred increased flexibility in the omega (Omega) loop. Amino acid changes that confer extended spectrum cephalosporinase activity to OXA-10-family beta-lactamases are concerning, given the rising reliance on novel beta-lactam/beta-lactamase inhibitor combinations, such as ceftolozane-tazobactam and ceftazidime-avibactam, to treat MDR P. aeruginosa infections. | |||
Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family beta-Lactamase from Pseudomonas aeruginosa.,Pincus NB, Rosas-Lemus M, Gatesy SWM, Bertucci HK, Brunzelle JS, Minasov G, Shuvalova LA, Lebrun-Corbin M, Satchell KJF, Ozer EA, Hauser AR, Bachta KER Antimicrob Agents Chemother. 2022 Oct 18;66(10):e0098522. doi: , 10.1128/aac.00985-22. Epub 2022 Sep 21. PMID:36129295<ref>PMID:36129295</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7n1m" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||