4EYL
Crystal structure of NDM-1 bound to hydrolyzed meropenem
Summary for 4EYL
| Entry DOI | 10.2210/pdb4eyl/pdb |
| Related | 3Q6X 3SPU 4EXY 4EY2 4EYB 4EYF 4EYL |
| Descriptor | Beta-lactamase NDM-1, (2S)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-3-methyl-2H-pyrro le-5-carboxylic acid, ZINC ION, ... (4 entities in total) |
| Functional Keywords | metallo-beta-lactamase, antibiotic, hydrolase-antibiotic complex, hydrolase/antibiotic |
| Biological source | Klebsiella pneumoniae |
| Cellular location | Periplasm : C7C422 |
| Total number of polymer chains | 2 |
| Total formula weight | 58539.99 |
| Authors | Strynadka, N.C.J.,King, D.T. (deposition date: 2012-05-01, release date: 2012-08-08, Last modification date: 2024-02-28) |
| Primary citation | King, D.T.,Worrall, L.J.,Gruninger, R.,Strynadka, N.C. New Delhi Metallo-Beta-Lactamase: Structural Insights into Beta-Lactam Recognition and Inhibition J.Am.Chem.Soc., 134:11362-11365, 2012 Cited by PubMed Abstract: The β-lactam antibiotics have long been a cornerstone for the treatment of bacterial disease. Recently, a readily transferable antibiotic resistance factor called the New Delhi metallo-β-lactamase-1 (NDM-1) has been found to confer enteric bacteria resistance to nearly all β-lactams, including the heralded carbapenems, posing a serious threat to human health. The crystal structure of NDM-1 bound to meropenem shows for the first time the molecular details of how carbapenem antibiotics are recognized by dizinc-containing metallo-β-lactamases. Additionally, product complex structures of hydrolyzed benzylpenicillin-, methicillin-, and oxacillin-bound NDM-1 have been solved to 1.8, 1.2, and 1.2 Å, respectively, and represent the highest-resolution structural data for any metallo-β-lactamase reported to date. Finally, we present the crystal structure of NDM-1 bound to the potent competitive inhibitor l-captopril, which reveals a unique binding mechanism. An analysis of the NDM-1 active site in these structures reveals key features important for the informed design of novel inhibitors of NDM-1 and other metallo-β-lactamases. PubMed: 22713171DOI: 10.1021/ja303579d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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