6rj7: Difference between revisions
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==Crystal structure of the 19F labelled OXA-48== | |||
<StructureSection load='6rj7' size='340' side='right'caption='[[6rj7]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rj7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RJ7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=K5H:'>K5H</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rj7 OCA], [http://pdbe.org/6rj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rj7 RCSB], [http://www.ebi.ac.uk/pdbsum/6rj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rj7 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial production of beta-lactamases with carbapenemase activity is a global health threat. The active sites of class D carbapenemases such as OXA-48, which is of major clinical importance, uniquely contain a carbamylated lysine residue which is essential for catalysis. Although there is significant interest in characterizing this post-translational modification, and it is a promising inhibition target, protein carbamylation is challenging to monitor in solution. We report the use of 19F-NMR spectroscopy to monitor the carbamylation state of 19F-labelled OXA-48. This method was used to investigate the interactions of OXA-48 with clinically used serine beta- lactamase inhibitors, including avibactam and vaborbactam. Crystallographic studies on 19F-labelled OXA-48 provide a structural rationale for the sensitivity of the 19F-label to active site interactions. The overall results demonstrate the use of 19F-NMR to monitor reversible covalent post-translational modifications. | |||
19F-NMR Monitoring of Reversible Protein Post-Translational Modifications: Class D beta-Lactamase Carbamylation and Inhibition.,van Groesen E, Lohans CT, Brem J, Aertker KM, Claridge TD, Schofield C Chemistry. 2019 Jul 16. doi: 10.1002/chem.201902529. PMID:31310409<ref>PMID:31310409</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rj7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Beta-lactamase]] | |||
[[Category: Large Structures]] | |||
[[Category: Brem, J]] | |||
[[Category: Lohans, C]] | |||
[[Category: Schofield, C]] | |||
[[Category: 19f labelling]] | |||
[[Category: Antibiotic resistance]] | |||
[[Category: Antimicrobial protein]] | |||
[[Category: Beta lactmase]] | |||
Revision as of 06:33, 31 July 2019
Crystal structure of the 19F labelled OXA-48
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