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==== | ==OXA-10 beta-lactamase with S64Dha modification and lysinoalanine crosslink== | ||
<StructureSection load='7b3r' size='340' side='right'caption='[[7b3r]]' scene=''> | <StructureSection load='7b3r' size='340' side='right'caption='[[7b3r]], [[Resolution|resolution]] 1.83Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7b3r]] 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=7B3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B3R FirstGlance]. <br> | ||
</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=7b3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b3r OCA], [https://pdbe.org/7b3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b3r RCSB], [https://www.ebi.ac.uk/pdbsum/7b3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b3r ProSAT]</span></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]] 1.83Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7b3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b3r OCA], [https://pdbe.org/7b3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b3r RCSB], [https://www.ebi.ac.uk/pdbsum/7b3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b3r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition. | |||
Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701<ref>PMID:35486701</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7b3r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Brem J]] | |||
[[Category: Lang PA]] | |||
[[Category: Schofield CJ]] | |||
Latest revision as of 15:21, 1 February 2024
OXA-10 beta-lactamase with S64Dha modification and lysinoalanine crosslinkOXA-10 beta-lactamase with S64Dha modification and lysinoalanine crosslink
Structural highlights
FunctionBLO10_PSEAI Hydrolyzes both carbenicillin and oxacillin. Publication Abstract from PubMedSignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition. Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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