2uyx

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{{Seed}}
 
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[[Image:2uyx.png|left|200px]]
 
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==metallo-beta-lactamase (1BC2) single point mutant D120S==
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The line below this paragraph, containing "STRUCTURE_2uyx", creates the "Structure Box" on the page.
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<StructureSection load='2uyx' size='340' side='right'caption='[[2uyx]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2uyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UYX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2uyx| PDB=2uyx | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2uyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyx OCA], [https://pdbe.org/2uyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uyx RCSB], [https://www.ebi.ac.uk/pdbsum/2uyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/2uyx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2uyx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Metallo-beta-lactamases are zinc-dependent hydrolases that inactivate beta-lactam antibiotics, rendering bacteria resistant to them. Asp-120 is fully conserved in all metallo-beta-lactamases and is central to catalysis. Several roles have been proposed for Asp-120, but so far there is no agreed consensus. We generated four site-specifically substituted variants of the enzyme BcII from Bacillus cereus as follows: D120N, D120E, D120Q, and D120S. Replacement of Asp-120 by other residues with very different metal ligating capabilities severely impairs the lactamase activity without abolishing metal binding to the mutated site. A kinetic study of these mutants indicates that Asp-120 is not the proton donor, nor does it play an essential role in nucleophilic activation. Spectroscopic and crystallographic analysis of D120S BcII, the least active mutant bearing the weakest metal ligand in the series, reveals that this enzyme is able to accommodate a dinuclear center and that perturbations in the active site are limited to the Zn2 site. It is proposed that the role of Asp-120 is to act as a strong Zn2 ligand, locating this ion optimally for substrate binding, stabilization of the development of a partial negative charge in the beta-lactam nitrogen, and protonation of this atom by a zinc-bound water molecule.
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===METALLO-BETA-LACTAMASE (1BC2) SINGLE POINT MUTANT D120S===
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Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity.,Llarrull LI, Fabiane SM, Kowalski JM, Bennett B, Sutton BJ, Vila AJ J Biol Chem. 2007 Jun 22;282(25):18276-85. Epub 2007 Apr 10. PMID:17426028<ref>PMID:17426028</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2uyx" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17426028}}, adds the Publication Abstract to the page
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17426028 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17426028}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2UYX is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYX OCA].
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==Reference==
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<ref group="xtra">PMID:17426028</ref><references group="xtra"/>
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[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Beta-lactamase]]
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[[Category: Large Structures]]
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[[Category: Bennett, B.]]
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[[Category: Bennett B]]
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[[Category: Fabiane, S M.]]
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[[Category: Fabiane SM]]
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[[Category: Kowalski, J M.]]
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[[Category: Kowalski JM]]
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[[Category: Larrull, L I.]]
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[[Category: Larrull LI]]
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[[Category: Sutton, B J.]]
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[[Category: Sutton BJ]]
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[[Category: Vila, A J.]]
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[[Category: Vila AJ]]
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[[Category: Antibiotic resistance]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Metallo beta- lactamase]]
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[[Category: Penicillinase]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:45:57 2009''
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Current revision

metallo-beta-lactamase (1BC2) single point mutant D120S

PDB ID 2uyx

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