4mss: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mss]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MSS FirstGlance]. <br> | <table><tr><td colspan='2'>[[4mss]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MSS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CZ:N-[(3S,4R,5R,6S)-4,5,6-TRIHYDROXYAZEPAN-3-YL]ACETAMIDE'>2CZ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CZ:N-[(3S,4R,5R,6S)-4,5,6-TRIHYDROXYAZEPAN-3-YL]ACETAMIDE'>2CZ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4mss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mss OCA], [https://pdbe.org/4mss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mss RCSB], [https://www.ebi.ac.uk/pdbsum/4mss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mss 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=4mss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mss OCA], [https://pdbe.org/4mss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mss RCSB], [https://www.ebi.ac.uk/pdbsum/4mss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mss ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 19:41, 20 September 2023
Crystal structure of Burkholderia cenocepacia family 3 glycoside hydrolase (NagZ) bound to (3S,4R,5R,6S)-3-acetamido-4,5,6-trihydroxyazepaneCrystal structure of Burkholderia cenocepacia family 3 glycoside hydrolase (NagZ) bound to (3S,4R,5R,6S)-3-acetamido-4,5,6-trihydroxyazepane
Structural highlights
FunctionPublication Abstract from PubMedAmpC beta-lactamase confers resistance to beta-lactam antibiotics in many Gram negative bacteria. Inducible expression of AmpC requires an N-acetylglucosaminidase termed NagZ. Here we describe the synthesis and characterization of hydroxyazepane inhibitors of NagZ. We find that these inhibitors enhance the susceptibility of clinically relevant Pseudomonas aeruginosa to beta-lactams. Selective trihydroxyazepane NagZ inhibitors increase sensitivity of Pseudomonas aeruginosa to beta-lactams.,Mondon M, Hur S, Vadlamani G, Rodrigues P, Tsybina P, Oliver A, Mark BL, Vocadlo DJ, Bleriot Y Chem Commun (Camb). 2013 Oct 29;49(93):10983-5. doi: 10.1039/c3cc46646a. PMID:24136176[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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