3SPU
apo NDM-1 Crystal Structure
Summary for 3SPU
| Entry DOI | 10.2210/pdb3spu/pdb |
| Descriptor | Beta-lactamase NDM-1, ZINC ION (3 entities in total) |
| Functional Keywords | alpha beta/beta alpha sandwich, hydrolase, beta lactam antibiotics, periplasmic space |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 5 |
| Total formula weight | 141813.08 |
| Authors | Strynadka, N.C.J.,King, D.T. (deposition date: 2011-07-03, release date: 2011-08-03, Last modification date: 2023-09-13) |
| Primary citation | King, D.,Strynadka, N. Crystal structure of New Delhi metallo-beta-lactamase reveals molecular basis for antibiotic resistance Protein Sci., 20:1484-1491, 2011 Cited by PubMed Abstract: β-Lactams are the most commonly prescribed class of antibiotics and have had an enormous impact on human health. Thus, it is disquieting that an enzyme called New Delhi metallo-β-lactamase-1 (NDM-1) can confer Enterobacteriaceae with nearly complete resistance to all β-lactam antibiotics including the carbapenams. We have determined the crystal structure of Klebsiella pneumoniae apo-NDM-1 to 2.1-Å resolution. From the structure, we see that NDM-1 has an expansive active site with a unique electrostatic profile, which we propose leads to a broader substrate specificity. In addition, NDM-1 undergoes important conformational changes upon substrate binding. These changes have not been previously observed in metallo-β-lactamase enzymes and may have a direct influence on substrate recognition and catalysis. PubMed: 21774017DOI: 10.1002/pro.697 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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