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| | <StructureSection load='5ggw' size='340' side='right'caption='[[5ggw]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='5ggw' size='340' side='right'caption='[[5ggw]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ggw]] 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=5GGW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GGW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ggw]] 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=5GGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GGW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.762Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ggw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ggw OCA], [https://pdbe.org/5ggw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ggw RCSB], [https://www.ebi.ac.uk/pdbsum/5ggw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ggw ProSAT]</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=5ggw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ggw OCA], [http://pdbe.org/5ggw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ggw RCSB], [http://www.ebi.ac.uk/pdbsum/5ggw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ggw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B7SNP8_ECOLX B7SNP8_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: An, Y J]] | + | [[Category: An YJ]] |
| - | [[Category: Cha, S S]] | + | [[Category: Cha SS]] |
| - | [[Category: Na, J H]] | + | [[Category: Na JH]] |
| - | [[Category: Class c]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
B7SNP8_ECOLX
Publication Abstract from PubMed
AmpC BER is an extended substrate spectrum class C beta-lactamase with a two-amino-acid insertion in the R2 loop compared with AmpC EC2. The crystal structures of AmpC BER (S64A mutant) and AmpC EC2 were determined. Structural comparison of the two proteins revealed that the insertion increases the conformational flexibility of the R2 loop. Two citrate molecules originating from the crystallization solution were observed in the active site of the S64A mutant. One citrate molecule makes extensive interactions with active-site residues that are highly conserved among class C beta-lactamases, whereas the other one is weakly bound. Based on this structural observation, it is demonstrated that citrate, a primary metabolite that is widely used as a food additive, is a competitive inhibitor of two class C beta-lactamases (AmpC BER and CMY-10). Consequently, the data indicate enhancement of the flexibility of the R2 loop as an operative strategy for molecular evolution of extended-spectrum class C beta-lactamases, and also suggest that the citrate scaffold is recognized by the active sites of class C beta-lactamases.
Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10.,Na JH, Cha SS Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):976-85. doi:, 10.1107/S2059798316011311. Epub 2016 Jul 28. PMID:27487828[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Na JH, Cha SS. Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10. Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):976-85. doi:, 10.1107/S2059798316011311. Epub 2016 Jul 28. PMID:27487828 doi:http://dx.doi.org/10.1107/S2059798316011311
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