4wz4
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='4wz4' size='340' side='right' caption='[[4wz4]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='4wz4' size='340' side='right' caption='[[4wz4]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4wz4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZ4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wz4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZ4 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3VU:{(3R)-6-[(3-AMINO-1,2,4-THIADIAZOL-5-YL)OXY]-1-HYDROXY-4,5-DIMETHYL-1,3-DIHYDRO-2,1-BENZOXABOROL-3-YL}ACETIC+ACID'>3VU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3VU:{(3R)-6-[(3-AMINO-1,2,4-THIADIAZOL-5-YL)OXY]-1-HYDROXY-4,5-DIMETHYL-1,3-DIHYDRO-2,1-BENZOXABOROL-3-YL}ACETIC+ACID'>3VU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wyy|4wyy]], [[4wz5|4wz5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wyy|4wyy]], [[4wz5|4wz5]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC, PA4110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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='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=4wz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wz4 OCA], [http://pdbe.org/4wz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wz4 RCSB], [http://www.ebi.ac.uk/pdbsum/4wz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wz4 ProSAT]</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=4wz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wz4 OCA], [http://pdbe.org/4wz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wz4 RCSB], [http://www.ebi.ac.uk/pdbsum/4wz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wz4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterially expressed beta-lactamases are rapidly eroding the clinical utility of the important beta-lactam class of antibacterials, significantly impairing our ability to fight serious bacterial infections. This paper describes a study of oxaborole-derived beta-lactamase inhibitors in which crystal structures and computational modeling aided in the rational design of analogues with improved spectrum of activity against class A, C, and D enzymes. Crystal structures of two of these inhibitors covalently bound to two different serine beta-lactamases, class C Pseudomonas aeruginosa AmpC and class D OXA-10, are described herein. Improved physicochemical properties as well as increased activity against an array of beta-lactamases resulted in substantial restoration of susceptibility to ceftazidime in Escherichia coli and Klebsiella pneumoniae. | ||
| + | |||
| + | 4,5-Disubstituted 6-Aryloxy-1,3-dihydrobenzo[c][1,2]oxaboroles Are Broad-Spectrum Serine beta-Lactamase Inhibitors.,McKinney DC, Zhou F, Eyermann CJ, Ferguson AD, Prince DB, Breen J, Giacobbe RA, Lahiri S, Verheijen JC ACS Infect Dis. 2015 Jul 10;1(7):310-6. doi: 10.1021/acsinfecdis.5b00031. Epub, 2015 Jun 18. PMID:27622821<ref>PMID:27622821</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4wz4" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase|Beta-lactamase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
| + | [[Category: Pseae]] | ||
[[Category: Ferguson, A D]] | [[Category: Ferguson, A D]] | ||
[[Category: Beta lactamase]] | [[Category: Beta lactamase]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
Revision as of 05:45, 25 April 2018
Crystal structure of P. aeruginosa AmpC
| |||||||||||
