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==Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 1 mM Zn(II)==
==Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 1 mM Zn(II)==
<StructureSection load='3knr' size='340' side='right' caption='[[3knr]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
<StructureSection load='3knr' size='340' side='right'caption='[[3knr]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3knr]] is a 4 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=3KNR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KNR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3knr]] is a 4 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=3KNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KNR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.71&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bvt|1bvt]], [[1bc2|1bc2]], [[3kns|3kns]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</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=3knr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3knr OCA], [https://pdbe.org/3knr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3knr RCSB], [https://www.ebi.ac.uk/pdbsum/3knr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3knr ProSAT]</span></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3knr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3knr OCA], [http://pdbe.org/3knr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3knr RCSB], [http://www.ebi.ac.uk/pdbsum/3knr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3knr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE]] Can hydrolyze carbapenem compounds.
[https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent beta-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such Zn(II)-cysteine interaction is an adaptive trait that tunes the metal binding affinity, thus enabling antibiotic resistance at restrictive Zn(II) concentrations.


Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.,Gonzalez JM, Meini MR, Tomatis PE, Martin FJ, Cricco JA, Vila AJ Nat Chem Biol. 2012 Jun 24. doi: 10.1038/nchembio.1005. PMID:22729148<ref>PMID:22729148</ref>
==See Also==
 
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3knr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 14579]]
[[Category: Bacillus cereus]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Gonzalez, J M]]
[[Category: Gonzalez JM]]
[[Category: Martin, F J.Medrano]]
[[Category: Medrano Martin FJ]]
[[Category: Vila, A J]]
[[Category: Vila AJ]]
[[Category: Antibiotic resistance]]
[[Category: Hydrolase]]
[[Category: Metal-binding]]
[[Category: Metallo-beta-lactamase]]
[[Category: Zn-dependent hydrolase]]
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