3kns: Difference between revisions
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==Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)== | |||
<StructureSection load='3kns' size='340' side='right' caption='[[3kns]], [[Resolution|resolution]] 1.58Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3kns]] is a 4 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=3KNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KNS 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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bvt|1bvt]], [[1bc2|1bc2]], [[3knr|3knr]]</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 Bacillus cereus])</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=3kns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kns OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kns RCSB], [http://www.ebi.ac.uk/pdbsum/3kns PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Gonzalez, J M | [[Category: Gonzalez, J M]] | ||
[[Category: Martin, F J.Medrano | [[Category: Martin, F J.Medrano]] | ||
[[Category: Vila, A J | [[Category: Vila, A J]] | ||
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 16:58, 18 December 2014
Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)
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