2m5c
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII== | |
| + | <StructureSection load='2m5c' size='340' side='right'caption='[[2m5c]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2m5c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M5C FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m5c OCA], [https://pdbe.org/2m5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m5c RCSB], [https://www.ebi.ac.uk/pdbsum/2m5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m5c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metallo-beta-lactamases, enzymes which inactivate beta-lactam antibiotics, are of increasing biological and clinical significance as a source of antibiotic resistance in pathogenic bacteria. We describe the high resolution solution NMR structures of the Bacillus cereus metallo-beta-lactamase, BcII, and of its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-beta-lactamases. This is the first reported solution structure of any metallo-beta-lactamase. There are differences between the solution structure of the free enzyme and previously reported crystal structures in the loops flanking the active site, which are important for substrate and inhibitor binding and catalysis. The binding of R-thiomandelic acid and the roles of active site residues are defined in detail. Changes in the enzyme structure upon inhibitor binding clarify the role of the mobile beta3-beta4 loop. Comparisons with other metallo-beta-lactamases highlight the roles of individual amino-acid residues in the active site and the beta3-beta4 loop in inhibitor binding and provide information on the basis of structure-activity relationships among metallo-beta-lactamase inhibitors. | ||
| - | + | Solution Structures of the Bacillus cereus Metallo-beta-Lactamase BcII and its Complex with the Broad Spectrum Inhibitor R-Thiomandelic Acid.,Karsisiotis AI, Damblon CF, Roberts GC Biochem J. 2013 Sep 24. PMID:24059435<ref>PMID:24059435</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2m5c" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus cereus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Damblon CF]] | ||
| + | [[Category: Karsisiotis AI]] | ||
| + | [[Category: Roberts GCK]] | ||
Current revision
Solution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII
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