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| | <StructureSection load='3v3r' size='340' side='right'caption='[[3v3r]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3v3r' size='340' side='right'caption='[[3v3r]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3v3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V3R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3v3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V3R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.898Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qpn|2qpn]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaGES-11, GES11 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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=3v3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3r OCA], [https://pdbe.org/3v3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3r RCSB], [https://www.ebi.ac.uk/pdbsum/3v3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3r ProSAT]</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=3v3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3r OCA], [https://pdbe.org/3v3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3r RCSB], [https://www.ebi.ac.uk/pdbsum/3v3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/C5HUY1_ACIBA C5HUY1_ACIBA] |
| - | GES-1 is a class A extended-spectrum beta-lactamase conferring resistance to penicillins, first-, second-generation cephalosporins and to ceftazidime. However, GES-1 poorly hydrolyzes aztreonam and cephamycins, and exhibits very low k(cat) values for carbapenems. Twenty-two GES variants have been discovered thus far, differing from each other by 1-3 amino acid substitutions that affect substrate specificity. GES-11 possesses a Gly243Ala substitution which seems to confer this variant an increased activity against aztreonam and ceftazidime. GES-12 differs from GES-11 by a single Thr237Ala substitution while GES-14 differs from GES-11 by the Gly170Ser mutation which is known to confer increased carbapenemase activity. GES-11 and GES-12 were kinetically characterized and compared with GES-1 and GES-14. Purified GES-11 and GES-12 showed strong activities against most tested beta-lactams with the exception of temocillin, cefoxitin and carbapenems. Both variants showed a significantly increased rate of hydrolysis of cefotaxime, ceftazidime and aztreonam. On the other hand, GES-11, GES-12 (and GES-14) variants all containing Ala243 exhibited increased susceptibility to classical inhibitors. The crystallographic structures of the GES-11 and GES-14 beta-lactamases were solved. The overall structures of GES-11 and GES-14 are similar to that of GES-1. The Gly243Ala substitution caused only subtle local rearrangements, notably in the typical carbapenemase disulfide bond. The active sites of GES-14 and GES-11 are very similar, the Gly170Ser substitution leading only to the formation of additional hydrogen bonds of the Ser residue with the hydrolytic water and the Glu166 residue.
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| - | | + | |
| - | Kinetic and crystallographic studies of extended spectrum GES-11, GES-12 and GES-14 beta-lactamases.,Delbruck H, Bogaerts P, Kupper MB, de Castro RR, Bennink S, Glupczynski Y, Galleni M, Hoffmann KM, Bebrone C Antimicrob Agents Chemother. 2012 Aug 20. PMID:22908160<ref>PMID:22908160</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3v3r" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aciba]] | + | [[Category: Acinetobacter baumannii]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bebrone, C]] | + | [[Category: Bebrone C]] |
| - | [[Category: Delbruck, H]] | + | [[Category: Delbruck H]] |
| - | [[Category: Hoffmann, K M.V]] | + | [[Category: Hoffmann KMV]] |
| - | [[Category: Beta lactamase fold]]
| + | |
| - | [[Category: Beta lactam]]
| + | |
| - | [[Category: Hydrolase]]
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