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{{STRUCTURE_4gzb|  PDB=4gzb  |  SCENE=  }}
===Crystal structure of native AmpC beta-lactamase from Pseudomonas aeruginosa PAO1===
{{ABSTRACT_PUBMED_23439634}}


==About this Structure==
==Crystal structure of native AmpC beta-lactamase from Pseudomonas aeruginosa PAO1==
[[4gzb]] 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=4GZB OCA].  
<StructureSection load='4gzb' size='340' side='right' caption='[[4gzb]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gzb]] 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=4GZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GZB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hbt|4hbt]], [[4hbu|4hbu]], [[4hef|4hef]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC, blaAmpC, 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='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=4gzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gzb OCA], [http://pdbe.org/4gzb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gzb RCSB], [http://www.ebi.ac.uk/pdbsum/4gzb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gzb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although beta-lactams have been the most effective class of antibacterial agents used in clinical practice for the past half century, their effectiveness on Gram-negative bacteria has been eroded due to the emergence and spread of beta-lactamase enzymes that are not affected by currently marketed beta-lactam/beta-lactamase inhibitor combinations. Avibactam is a novel, covalent, non-beta-lactam beta-lactamase inhibitor presently in clinical development in combination with either ceftaroline or ceftazidime. In vitro studies show that avibactam may restore the broad-spectrum activity of cephalosporins against class A, class C and some class D beta-lactamases. Here we describe the structure of two clinically important beta-lactamase enzymes bound to avibactam, the class A CTX-M-15 extended-spectrum beta-lactamase and class C Pseudomonas aeruginosa AmpC beta-lactamase, which together provide insight into the binding modes for the respective enzyme classes. The structure reveals a similar binding mode in both enzymes and thus provides a rationale for the broad-spectrum inhibitory activity of avibactam. Identification of the key residues surrounding the binding pocket allows for a better understanding of the potency of this scaffold. Finally, avibactam has recently been shown to be a reversible inhibitor and the structure provides insights into the mechanism of avibactam recyclization. Analysis of the ultra-high resolution CTX-M-15 structure suggests how the deacylation mechanism favors recyclization over hydrolysis.
 
Structural Insight into Potent Broad-spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC beta-lactamases.,Lahiri SD, Mangani S, Durand-Reville T, Benvenuti M, De Luca F, Sanyal G, Docquier JD Antimicrob Agents Chemother. 2013 Feb 25. PMID:23439634<ref>PMID:23439634</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gzb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase|Beta-lactamase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:023439634</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Pseae]]
[[Category: Pseae]]
[[Category: Benvenuti, M.]]
[[Category: Benvenuti, M]]
[[Category: Docquier, J D.]]
[[Category: Docquier, J D]]
[[Category: Luca, F De.]]
[[Category: Luca, F De]]
[[Category: Mangani, S.]]
[[Category: Mangani, S]]
[[Category: Antibiotic resistance]]
[[Category: Antibiotic resistance]]
[[Category: Beta-lactamase fold]]
[[Category: Beta-lactamase fold]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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