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6s0h
From Proteopedia
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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=6s0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0h OCA], [http://pdbe.org/6s0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s0h RCSB], [http://www.ebi.ac.uk/pdbsum/6s0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0h ProSAT]</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=6s0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0h OCA], [http://pdbe.org/6s0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s0h RCSB], [http://www.ebi.ac.uk/pdbsum/6s0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Multi-drug resistance among Gram-negative bacteria is a major global public health threat. Metallo-beta-lactamases (MBLs) target the most widely-used antibiotic class, the beta-lactams, including the most recent-generation carbapenems. Interspecies spread renders these enzymes a serious clinical threat and there are no clinically-available inhibitors. We present crystal structures of IMP-13, a structurally-uncharacterized MBL from Gram-negative Pseudomonas aerugionasa found in clinical outbreaks globally, and characterize the binding using solution NMR-spectroscopy and molecular-dynamics simulations. Crystal structures of apo IMP-13 and bound to four clinically-relevant carbapenem antibiotics (doripenem, ertapenem, imipenem and meropenem) are presented. Active site plasticity and the active-site loop, where a tryptophan residue stabilizes the antibiotic core scaffold, are essential to the substrate-binding mechanism. The conserved carbapenem scaffold plays the most significant role in IMP-13 binding, explaining the broad substrate specificity. The observed plasticity and substrate-locking mechanism provide opportunities for rational drug design of novel metallo-beta-lactamase inhibitors, essential in the fight against antibiotic resistance. | ||
| + | |||
| + | Structure and molecular recognition mechanism of IMP-13 metallo-beta-lactamase.,Softley CA, Zak KM, Bostock MJ, Fino R, Zhou RX, Kolonko M, Mejdi-Nitiu R, Meyer H, Sattler M, Popowicz GM Antimicrob Agents Chemother. 2020 Mar 23. pii: AAC.00123-20. doi:, 10.1128/AAC.00123-20. PMID:32205343<ref>PMID:32205343</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6s0h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:05, 29 April 2020
Structure of IMP-13 metallo-beta-lactamase complexed with hydrolysed doripenem
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