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| | <StructureSection load='5chj' size='340' side='right'caption='[[5chj]], [[Resolution|resolution]] 1.36Å' scene=''> | | <StructureSection load='5chj' size='340' side='right'caption='[[5chj]], [[Resolution|resolution]] 1.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5chj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5CHJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5chj]] is a 2 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=5CHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CHJ FirstGlance]. <br> |
| | </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=SM2:(1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC+ACID'>SM2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | | </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=SM2:(1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC+ACID'>SM2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cgs|5cgs]], [[5cgw|5cgw]], [[5cgx|5cgx]], [[5chm|5chm]]</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=5chj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chj OCA], [https://pdbe.org/5chj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5chj RCSB], [https://www.ebi.ac.uk/pdbsum/5chj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5chj ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fox-4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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://proteopedia.org/fgij/fg.htm?mol=5chj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chj OCA], [http://pdbe.org/5chj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5chj RCSB], [http://www.ebi.ac.uk/pdbsum/5chj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5chj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9L387_ECOLX Q9L387_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Almo, S C]] | + | [[Category: Almo SC]] |
| - | [[Category: Lefurgy, S]] | + | [[Category: Lefurgy S]] |
| - | [[Category: Malashkevich, V N]] | + | [[Category: Malashkevich VN]] |
| - | [[Category: Toro, R]] | + | [[Category: Toro R]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q9L387_ECOLX
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 < 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lefurgy ST, Caselli E, Taracila MA, Malashkevich VN, Biju B, Papp-Wallace KM, Bonanno JB, Prati F, Almo SC, Bonomo RA. Structures of FOX-4 Cephamycinase in Complex with Transition-State Analog Inhibitors. Biomolecules. 2020 Apr 27;10(5). pii: biom10050671. doi: 10.3390/biom10050671. PMID:32349291 doi:http://dx.doi.org/10.3390/biom10050671
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