1dxk

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[[Image:1dxk.png|left|200px]]
 
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==Metallo-beta-lactamase from Bacillus cereus 569/H/9 C168S mutant==
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The line below this paragraph, containing "STRUCTURE_1dxk", creates the "Structure Box" on the page.
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<StructureSection load='1dxk' size='340' side='right'caption='[[1dxk]], [[Resolution|resolution]] 1.85&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'>[[1dxk]] 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=1DXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DXK 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]] 1.85&#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=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1dxk| PDB=1dxk | 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=1dxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dxk OCA], [https://pdbe.org/1dxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dxk RCSB], [https://www.ebi.ac.uk/pdbsum/1dxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dxk 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/dx/1dxk_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=1dxk 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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Beta-lactamases are involved in bacterial resistance. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are becoming thus of major clinical importance. Despite the availability of Zn-beta-lactamase X-ray structures their mechanism of action is still unclear. One puzzling observation is the presence of one or two zincs in the active site. To aid in assessing the role of zinc content in beta-lactam hydrolysis, the replacement by Ser of the zinc-liganding residue Cys168 in the Zn-beta-lactamase from Bacillus cereus strain 569/H/9 was carried out: the mutant enzyme (C168S) is inactive in the mono-Zn form, but active in the di-Zn form. The structure of the mono-Zn form of the C168S mutant has been determined at 1.85 A resolution. Ser168 occupies the same position as Cys168 in the wild-type enzyme. The protein residues mostly affected by the mutation are Asp90-Arg91 and His210. A critical factor for the activity of the mono-Zn species is the distance between Asp90 and the Zn ion, which is controlled by Arg91: a slight movement of Asp90 impairs catalysis. The evolution of a large superfamily including Zn-beta-lactamases suggests that they may not all share the same mechanism.
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===METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9 C168S MUTANT===
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Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.,Chantalat L, Duee E, Galleni M, Frere JM, Dideberg O Protein Sci. 2000 Jul;9(7):1402-6. PMID:10933508<ref>PMID:10933508</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 1dxk" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10933508}}, 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 10933508 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10933508}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1dxk]] is a 1 chain structure with 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=1DXK OCA].
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==Reference==
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<ref group="xtra">PMID:10933508</ref><ref group="xtra">PMID:9761898</ref><ref group="xtra">PMID:7588620</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: Chantalat, L.]]
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[[Category: Chantalat L]]
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[[Category: Dideberg, O.]]
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[[Category: Dideberg O]]
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[[Category: Duee, E.]]
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[[Category: Duee E]]
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[[Category: Hydrolase]]
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[[Category: Metallo beta-lactamase]]
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[[Category: Zinc]]
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Current revision

Metallo-beta-lactamase from Bacillus cereus 569/H/9 C168S mutant

PDB ID 1dxk

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