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3i0v

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{{Seed}}
 
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[[Image:3i0v.png|left|200px]]
 
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<!--
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==Bacillus cereus metallo-beta-lactamase: apo form==
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The line below this paragraph, containing "STRUCTURE_3i0v", creates the "Structure Box" on the page.
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<StructureSection load='3i0v' size='340' side='right'caption='[[3i0v]], [[Resolution|resolution]] 1.60&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'>[[3i0v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I0V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3I0V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
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-->
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bvt|1bvt]], [[1bc2|1bc2]], [[3i11|3i11]], [[3i13|3i13]], [[3i14|3i14]], [[3i15|3i15]]</td></tr>
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{{STRUCTURE_3i0v| PDB=3i0v | SCENE= }}
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3i0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i0v OCA], [http://pdbe.org/3i0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i0v RCSB], [http://www.ebi.ac.uk/pdbsum/3i0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i0v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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/i0/3i0v_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=3i0v 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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Subclass B1 beta-lactamases are Zn(II)-dependent hydrolases that confer bacterial resistance to most clinically useful beta-lactam antibiotics. The enzyme BcII from Bacillus cereus is a prototypical enzyme that belongs to this group, the first Zn(II)-dependent beta-lactamase to be discovered. Crucial aspects of the BcII catalytic mechanism and metal binding mode have been assessed mostly on the Co(II)-substituted surrogate. Here we report a high-resolution structure of Co(II)-BcII, revealing a metal coordination geometry identical to that of the native zinc enzyme. In addition, a high-resolution structure of the apoenzyme, together with structures with different degrees of metal occupancy and oxidation levels of a conserved Cys ligand, discloses a considerable mobility of two loops containing four metal ligands (namely, regions His116-Arg121 and Gly219-Cys221). This flexibility is expected to assist in the structural rearrangement of the metal sites during catalytic turnover, which, along with the coordination geometry adaptability of Zn(II) ions, grants the interaction with a variety of substrates, a characteristic feature of B1 metallo-beta-lactamases.
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===Bacillus cereus metallo-beta-lactamase: apo form===
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Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .,Gonzalez JM, Buschiazzo A, Vila AJ Biochemistry. 2010 Sep 14;49(36):7930-8. PMID:20677753<ref>PMID:20677753</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 3i0v" style="background-color:#fffaf0;"></div>
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<!--
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20677753}}, 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 20677753 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_20677753}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Atcc 14579]]
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3I0V 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=3I0V OCA].
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==Reference==
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<ref group="xtra">PMID:20677753</ref><references group="xtra"/>
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[[Category: Bacillus cereus]]
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[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
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[[Category: Buschiazzo, A.]]
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[[Category: Large Structures]]
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[[Category: Gonzalez, J M.]]
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[[Category: Buschiazzo, A]]
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[[Category: Vila, A J.]]
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[[Category: Gonzalez, J M]]
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[[Category: Vila, A J]]
[[Category: Antibiotic resistance]]
[[Category: Antibiotic resistance]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Metallo-beta-lactamase superfamily]]
[[Category: Metallo-beta-lactamase superfamily]]
[[Category: Zn-dependent hydrolase]]
[[Category: Zn-dependent hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 20 06:10:58 2010''
 

Current revision

Bacillus cereus metallo-beta-lactamase: apo form

PDB ID 3i0v

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