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2wki
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2wki is ON HOLD Authors: Vercheval, L., Bauvois, C., Kerff, F., Sauvage, E., Guiet, R., Charlier, P., Galleni, M. Description: Crystal structure of...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the OXA-10 K70C mutant at pH 7.0== | |
| + | <StructureSection load='2wki' size='340' side='right'caption='[[2wki]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2wki]] 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=2WKI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WKI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wki OCA], [https://pdbe.org/2wki PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wki RCSB], [https://www.ebi.ac.uk/pdbsum/2wki PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wki ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wk/2wki_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wki ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The activity of class D beta-lactamases is dependent on Lys70 carboxylation in the active site. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also by the V117T substitution. Val117 is a strictly conserved hydrophobic residue located in the active site. In addition, inhibition of class D beta-lactamases by chloride ions is due to a competition between the side chain carboxylate of the modified Lys70 and chloride ions. Determination of the individual kinetic constants shows that the deacylation of the acyl-enzyme is the rate-limiting step for the wild-type OXA-10 beta-lactamase. | ||
| - | + | Three factors that modulate the activity of class D beta-lactamases and interfere with the post-translational carboxylation of Lys70.,Vercheval L, Bauvois C, di Paolo A, Borel F, Ferrer JL, Sauvage E, Matagne A, Frere JM, Charlier P, Galleni M, Kerff F Biochem J. 2010 Nov 25;432(3):495-504. PMID:21108605<ref>PMID:21108605</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2wki" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa]] | ||
| + | [[Category: Bauvois C]] | ||
| + | [[Category: Charlier P]] | ||
| + | [[Category: Galleni M]] | ||
| + | [[Category: Guiet R]] | ||
| + | [[Category: Kerff F]] | ||
| + | [[Category: Sauvage E]] | ||
| + | [[Category: Vercheval L]] | ||
Current revision
Crystal structure of the OXA-10 K70C mutant at pH 7.0
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