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==CRYSTAL STRUCTURE OF Fox-4 cephamycinase complexed with ceftazidime BATSI (LP06)==
==CRYSTAL STRUCTURE OF Fox-4 cephamycinase complexed with ceftazidime BATSI (LP06)==
<StructureSection load='5chm' size='340' side='right' caption='[[5chm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5chm' size='340' side='right'caption='[[5chm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5chm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHM FirstGlance]. <br>
<table><tr><td colspan='2'>[[5chm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CHM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CB4:PINACOL[[2-AMINO-ALPHA-(1-CARBOXY-1-METHYLETHOXYIMINO)-4-THIAZOLEACETYL]AMINO]METHANEBORONATE'>CB4</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cgs|5cgs]], [[5cgw|5cgw]], [[5cgx|5cgx]], [[5chj|5chj]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CB4:PINACOL[[2-AMINO-ALPHA-(1-CARBOXY-1-METHYLETHOXYIMINO)-4-THIAZOLEACETYL]AMINO]METHANEBORONATE'>CB4</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5chm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chm OCA], [https://pdbe.org/5chm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5chm RCSB], [https://www.ebi.ac.uk/pdbsum/5chm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5chm 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=5chm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chm OCA], [http://pdbe.org/5chm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5chm RCSB], [http://www.ebi.ac.uk/pdbsum/5chm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5chm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9L387_ECOLX Q9L387_ECOLX]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Boronic acid transition-state analog inhibitors (BATSIs) are partners with beta-lactam antibiotics for the treatment of complex bacterial infections. Herein, microbiological, biochemical, and structural findings on four BATSIs with the FOX-4 cephamycinase, a class C beta-lactamase that rapidly hydrolyzes cefoxitin, are revealed. FOX-4 is an extended-spectrum class C cephalosporinase that demonstrates conformational flexibility when complexed with certain ligands. Like other beta-lactamases of this class, studies on FOX-4 reveal important insights into structure-activity relationships. We show that SM23, a BATSI, shows both remarkable flexibility and affinity, binding similarly to other beta-lactamases, yet retaining an IC50 value &lt; 0.1 muM. Our analyses open up new opportunities for the design of novel transition-state analogs of class C enzymes.
Structures of FOX-4 Cephamycinase in Complex with Transition-State Analog Inhibitors.,Lefurgy ST, Caselli E, Taracila MA, Malashkevich VN, Biju B, Papp-Wallace KM, Bonanno JB, Prati F, Almo SC, Bonomo RA Biomolecules. 2020 Apr 27;10(5). pii: biom10050671. doi: 10.3390/biom10050671. PMID:32349291<ref>PMID:32349291</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5chm" style="background-color:#fffaf0;"></div>
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Escherichia coli]]
[[Category: Almo, S C]]
[[Category: Large Structures]]
[[Category: Lefurgy, S]]
[[Category: Almo SC]]
[[Category: Malashkevich, V N]]
[[Category: Lefurgy S]]
[[Category: Toro, R]]
[[Category: Malashkevich VN]]
[[Category: Hydrolase]]
[[Category: Toro R]]
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