7keq: Difference between revisions
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New page: '''Unreleased structure''' The entry 7keq is ON HOLD until Paper Publication Authors: Smith, C.A., Vakulenko, S.B., Stewart, N.K., Toth, M. Description: avibactam-CDD-1 6 minute comple... |
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==avibactam-CDD-1 6 minute complex== | |||
<StructureSection load='7keq' size='340' side='right'caption='[[7keq]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7keq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KEQ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FYG:(2S,5R)-7-oxo-6-(sulfooxy)-1,6-diazabicyclo[3.2.1]octane-2-carboxamide'>FYG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NXL:(2S,5R)-1-FORMYL-5-[(SULFOOXY)AMINO]PIPERIDINE-2-CARBOXAMIDE'>NXL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaR1_4, blaR1_1, E5F39_11445, SAMEA2239407_03320, SAMEA3374989_01677 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=7keq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7keq OCA], [https://pdbe.org/7keq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7keq RCSB], [https://www.ebi.ac.uk/pdbsum/7keq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7keq ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Avibactam is a potent diazobicyclooctane inhibitor of class A and C beta-lactamases. The inhibitor also exhibits variable activity against some class D enzymes from Gram-negative bacteria; however, its interaction with recently discovered class D beta-lactamases from Gram-positive bacteria has not been studied. Here, we describe microbiological, kinetic, and mass spectrometry studies of the interaction of avibactam with CDD-1, a class D beta-lactamase from the clinically important pathogen Clostridioides difficile, and show that avibactam is a potent irreversible mechanism-based inhibitor of the enzyme. X-ray crystallographic studies at three time-points demonstrate the rapid formation of a stable CDD-1-avibactam acyl-enzyme complex and highlight differences in the anchoring of the inhibitor by class D enzymes from Gram-positive and Gram-negative bacteria. | |||
Inhibition of the Clostridioides difficile Class D beta-Lactamase CDD-1 by Avibactam.,Stewart NK, Toth M, Stasyuk A, Lee M, Smith CA, Vakulenko SB ACS Infect Dis. 2021 Jan 3. doi: 10.1021/acsinfecdis.0c00714. PMID:33390002<ref>PMID:33390002</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Smith, C | <div class="pdbe-citations 7keq" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus difficilis hall and o'toole 1935]] | |||
[[Category: Beta-lactamase]] | |||
[[Category: Large Structures]] | |||
[[Category: Smith, C A]] | |||
[[Category: Stewart, N K]] | |||
[[Category: Toth, M]] | [[Category: Toth, M]] | ||
[[Category: Vakulenko, S | [[Category: Vakulenko, S B]] | ||
[[Category: | [[Category: Antibiotic resistance]] | ||
[[Category: Gram-positive]] | |||
[[Category: Hydrolase]] | |||
[[Category: Hydrolase-inhibitor complex]] | |||
[[Category: Inhibitor]] | |||
[[Category: Mutant]] | |||
Latest revision as of 12:28, 26 May 2021
avibactam-CDD-1 6 minute complexavibactam-CDD-1 6 minute complex
Structural highlights
Publication Abstract from PubMedAvibactam is a potent diazobicyclooctane inhibitor of class A and C beta-lactamases. The inhibitor also exhibits variable activity against some class D enzymes from Gram-negative bacteria; however, its interaction with recently discovered class D beta-lactamases from Gram-positive bacteria has not been studied. Here, we describe microbiological, kinetic, and mass spectrometry studies of the interaction of avibactam with CDD-1, a class D beta-lactamase from the clinically important pathogen Clostridioides difficile, and show that avibactam is a potent irreversible mechanism-based inhibitor of the enzyme. X-ray crystallographic studies at three time-points demonstrate the rapid formation of a stable CDD-1-avibactam acyl-enzyme complex and highlight differences in the anchoring of the inhibitor by class D enzymes from Gram-positive and Gram-negative bacteria. Inhibition of the Clostridioides difficile Class D beta-Lactamase CDD-1 by Avibactam.,Stewart NK, Toth M, Stasyuk A, Lee M, Smith CA, Vakulenko SB ACS Infect Dis. 2021 Jan 3. doi: 10.1021/acsinfecdis.0c00714. PMID:33390002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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