5j8x: Difference between revisions
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==CRYSTAL STRUCTURE OF E. COLI PBP5 WITH 2C== | |||
<StructureSection load='5j8x' size='340' side='right'caption='[[5j8x]], [[Resolution|resolution]] 2.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5j8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J8X 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]] 2.53Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OK3:(R)-3-(4-(AMINOMETHYL)BENZAMIDO)-8-CARBOXY-2,2-DIHYDROXY-3,4-DIHYDRO-2H-BENZO[E][1,2]OXABORININ-2-UIDE'>OK3</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=5j8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8x OCA], [https://pdbe.org/5j8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j8x RCSB], [https://www.ebi.ac.uk/pdbsum/5j8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DACA_ECOLI DACA_ECOLI] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-Lactamases enable resistance to almost all beta-lactam antibiotics. Pioneering work revealed that acyclic boronic acids can act as 'transition state analogue' inhibitors of nucleophilic serine enzymes, including serine-beta-lactamases. Here we report biochemical and biophysical analyses revealing that cyclic boronates potently inhibit both nucleophilic serine and zinc-dependent beta-lactamases by a mechanism involving mimicking of the common tetrahedral intermediate. Cyclic boronates also potently inhibit the non-essential penicillin-binding protein PBP 5 by the same mechanism of action. The results open the way for development of dual action inhibitors effective against both serine- and metallo-beta-lactamases, and which could also have antimicrobial activity through inhibition of PBPs. | |||
Structural basis of metallo-beta-lactamase, serine-beta-lactamase and penicillin-binding protein inhibition by cyclic boronates.,Brem J, Cain R, Cahill S, McDonough MA, Clifton IJ, Jimenez-Castellanos JC, Avison MB, Spencer J, Fishwick CW, Schofield CJ Nat Commun. 2016 Aug 8;7:12406. doi: 10.1038/ncomms12406. PMID:27499424<ref>PMID:27499424</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5j8x" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Brem J]] | |||
[[Category: Cain R]] | |||
[[Category: Clifton IJ]] | |||
[[Category: Fishwick CWG]] | |||
[[Category: McDonough MA]] | |||
[[Category: Schofield CJ]] | |||
Latest revision as of 10:54, 6 September 2023
CRYSTAL STRUCTURE OF E. COLI PBP5 WITH 2C
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