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| | <StructureSection load='2rl3' size='340' side='right'caption='[[2rl3]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2rl3' size='340' side='right'caption='[[2rl3]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rl3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RL3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rl3]] is a 2 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=2RL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RL3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hp6|2hp6]], [[2hp9|2hp9]], [[2hpb|2hpb]], [[2hp5|2hp5]], [[1k4f|1k4f]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pse2, oxa10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2rl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rl3 OCA], [https://pdbe.org/2rl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rl3 RCSB], [https://www.ebi.ac.uk/pdbsum/2rl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rl3 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=2rl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rl3 OCA], [https://pdbe.org/2rl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rl3 RCSB], [https://www.ebi.ac.uk/pdbsum/2rl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rl3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI]] Hydrolyzes both carbenicillin and oxacillin.
| + | [https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Charlier, P]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Frere, J M]] | + | [[Category: Charlier P]] |
| - | [[Category: Galleni, M]] | + | [[Category: Frere J-M]] |
| - | [[Category: Guiet, R]] | + | [[Category: Galleni M]] |
| - | [[Category: Herman, R]] | + | [[Category: Guiet R]] |
| - | [[Category: Kerff, F]] | + | [[Category: Herman R]] |
| - | [[Category: Sauvage, E]] | + | [[Category: Kerff F]] |
| - | [[Category: Vercheval, L]] | + | [[Category: Sauvage E]] |
| - | [[Category: Antibiotic resistance]]
| + | [[Category: Vercheval L]] |
| - | [[Category: Carboxylated lysine]]
| + | |
| - | [[Category: Class d beta-lactamase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Oxa-10]]
| + | |
| Structural highlights
Function
BLO10_PSEAI Hydrolyzes both carbenicillin and oxacillin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The catalytic efficiency of class D OXA-10 beta-lactamase depends critically on an unusual carboxylated lysine as the general base residue for both the enzyme acylation and deacylation steps of catalysis. Evidence is presented that the interaction between the indole group of Trp154 and the carboxylated lysine is essential for the stability of the post-translationally modified Lys70. Substitution of Trp154 by Gly, Ala or Phe yielded non carboxylated enzymes which displayed poor catalytic efficiencies and reduced stability when compared to the wild type OXA-10. The W154H mutant was partially carboxylated. In addition, the maximum values of kcat and kcat/KM were shifted toward pH 7 indicating that the carboxylation state of Lys70 is dependent on the protonation level of the histidine. A comparison of the three dimensional structures of the different proteins also indicated that the Trp154 mutations did not modify the overall structures of OXA-10 but induced an increased flexibility of the omega-loop in the active site. Finally, the deacylation impaired W154A mutant was used to determine the structure of the acyl-enzyme complex with benzylpenicillin. These results indicate a role of the Lys70 carboxylation during the deacylation step and emphasize the importance of Trp154 for the ideal positioning of active site residues leading to an optimum activity.
Critical role of Tryptophan 154 for the activity and stability of class D beta-lactamases.,Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frere JM, Charlier P, Galleni M, Kerff F Biochemistry. 2009 Oct 27. PMID:19860471[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frere JM, Charlier P, Galleni M, Kerff F. Critical role of Tryptophan 154 for the activity and stability of class D beta-lactamases. Biochemistry. 2009 Oct 27. PMID:19860471 doi:10.1021/bi901548c
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