View source for 6s1s


==Crystal structure of AmpC from Pseudomonas aeruginosa in complex with [3-(2-carboxyvinyl)phenyl]boronic acid] inhibitor==
<StructureSection load='6s1s' size='340' side='right'caption='[[6s1s]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6s1s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S1S 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]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KRT:(~{E})-3-[3-(dihydroxyboranyl)phenyl]prop-2-enoic+acid'>KRT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6s1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s1s OCA], [https://pdbe.org/6s1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s1s RCSB], [https://www.ebi.ac.uk/pdbsum/6s1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s1s ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q541D8_PSEAI Q541D8_PSEAI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Worldwide dissemination of pathogens resistant to almost all available antibiotics represent a real problem preventing efficient treatment of infectious diseases. Among antimicrobial used in therapy, beta-lactam antibiotics represent 40% thus playing a crucial role in the management of infections treatment. We report a small series of phenylboronic acids derivatives (BAs) active against class A carbapenemases KPC-2 and GES-5, and class C cephalosporinases AmpC. The inhibitory profile of our BAs against class A and C was investigated by means of molecular docking, enzyme kinetics and X-ray crystallography. We were interested in the mechanism of recognition among class A and class C to direct the design of broad serine beta-Lactamases (SBLs) inhibitors. Molecular modeling calculations vs GES-5 and crystallographic studies vs AmpC reasoned, respectively, the ortho derivative 2 and the meta derivative 3 binding affinity. The ability of our BAs to protect beta-lactams from BLs hydrolysis was determined in biological assays conducted against clinical strains: Fractional inhibitory concentration index (FICI) tests confirmed their ability to be synergic with beta-lactams thus restoring susceptibility to meropenem. Considering the obtained results and the lack of cytotoxicity, our derivatives represent validated probe for the design of SBLs inhibitors.

Phenylboronic Acids Probing Molecular Recognition against Class A and Class C beta-lactamases.,Linciano P, Vicario M, Kekez I, Bellio P, Celenza G, Martin-Blecua I, Blazquez J, Cendron L, Tondi D Antibiotics (Basel). 2019 Sep 30;8(4). pii: antibiotics8040171. doi:, 10.3390/antibiotics8040171. PMID:31574990<ref>PMID:31574990</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6s1s" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Bellio P]]
[[Category: Blazquez J]]
[[Category: Celenza G]]
[[Category: Cendron L]]
[[Category: Kekez I]]
[[Category: Tondi D]]
[[Category: Tosoni E]]
[[Category: Vicario M]]