3i13

<table><tr><td colspan='2'>[[3i13]] 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=3I13 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3I13 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]], [[3i0v|3i0v]], [[3i11|3i11]], [[3i14|3i14]], [[3i15|3i15]]</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://proteopedia.org/fgij/fg.htm?mol=3i13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i13 OCA], [http://pdbe.org/3i13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i13 RCSB], [http://www.ebi.ac.uk/pdbsum/3i13 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i13 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE]] Can hydrolyze carbapenem compounds.

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 14579]]

[[Category: Beta-lactamase]]

[[Category: Buschiazzo, A]]

[[Category: Gonzalez, J M]]

[[Category: Vila, A J]]

[[Category: Zn-dependent hydrolase]]