5nbk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NDM-1 metallo-beta-lactamase: a parsimonious interpretation of the diffraction data== | |
| + | <StructureSection load='5nbk' size='340' side='right' caption='[[5nbk]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5nbk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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">[[5a5z|5a5z]]</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=5nbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbk OCA], [http://pdbe.org/5nbk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbk RCSB], [http://www.ebi.ac.uk/pdbsum/5nbk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BLAN1_KLEPN BLAN1_KLEPN]] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.  | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Resistance to beta-lactam antibiotics can be mediated by metallo-beta-lactamase enzymes (MBLs). An MBL inhibitor could restore the effectiveness of beta-lactams. We report on the evaluation of approved thiol-containing drugs as inhibitors of NDM-1, VIM-1, and IMP-7. Drugs were assessed by a novel assay using a purchasable fluorescent substrate and thermal shift. Best compounds were tested in antimicrobial susceptibility assay. Using these orthogonal screening methods, we identified drugs that restored the activity of imipenem. | ||
| - | + | Approved Drugs Containing Thiols as Inhibitors of Metallo-beta-lactamases: Strategy To Combat Multidrug-Resistant Bacteria.,Klingler FM, Wichelhaus TA, Frank D, Cuesta-Bernal J, El-Delik J, Muller HF, Sjuts H, Gottig S, Koenigs A, Pos KM, Pogoryelov D, Proschak E J Med Chem. 2015 Apr 23;58(8):3626-30. doi: 10.1021/jm501844d. Epub 2015 Apr 13. PMID:25815530<ref>PMID:25815530</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5nbk" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category:  | + | <references/> | 
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-lactamase]] | ||
| [[Category: Jaskolski, M]] | [[Category: Jaskolski, M]] | ||
| - | [[Category: Raczynska, J | + | [[Category: Minor, W]] | 
| + | [[Category: Raczynska, J E]] | ||
| + | [[Category: Shabalin, I G]] | ||
| + | [[Category: Wlodawer, A]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Metallo-beta-lactamase]] | ||
| + | [[Category: Ndm-1]] | ||
Revision as of 07:36, 3 October 2018
NDM-1 metallo-beta-lactamase: a parsimonious interpretation of the diffraction data
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