3SBL
Crystal Structure of New Delhi Metal-beta-lactamase-1 from Klebsiella pneumoniae
Summary for 3SBL
| Entry DOI | 10.2210/pdb3sbl/pdb |
| Related | 3RKJ 3RKK |
| Descriptor | Beta-lactamase NDM-1, CITRIC ACID (3 entities in total) |
| Functional Keywords | structural genomics, psi-biology, midwest center for structural genomics, mcsg, alpha-beta structure, hydrolase, structures of mtb proteins conferring susceptibility to known mtb inhibitors, mtbi |
| Biological source | Klebsiella pneumoniae |
| Cellular location | Periplasm (Potential): C7C422 |
| Total number of polymer chains | 1 |
| Total formula weight | 25292.28 |
| Authors | Kim, Y.,Tesar, C.,Jedrzejczak, R.,Babnigg, J.,Binkowski, T.A.,Mire, J.,Sacchettini, J.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG),Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI) (deposition date: 2011-06-05, release date: 2011-06-29, Last modification date: 2023-09-13) |
| Primary citation | Kim, Y.,Tesar, C.,Mire, J.,Jedrzejczak, R.,Binkowski, A.,Babnigg, G.,Sacchettini, J.,Joachimiak, A. Structure of Apo- and Monometalated Forms of NDM-1 A Highly Potent Carbapenem-Hydrolyzing Metallo-beta-Lactamase Plos One, 6:e24621-e24621, 2011 Cited by PubMed Abstract: The New Delhi Metallo-β-lactamase (NDM-1) gene makes multiple pathogenic microorganisms resistant to all known β-lactam antibiotics. The rapid emergence of NDM-1 has been linked to mobile plasmids that move between different strains resulting in world-wide dissemination. Biochemical studies revealed that NDM-1 is capable of efficiently hydrolyzing a wide range of β-lactams, including many carbapenems considered as "last resort" antibiotics. The crystal structures of metal-free apo- and monozinc forms of NDM-1 presented here revealed an enlarged and flexible active site of class B1 metallo-β-lactamase. This site is capable of accommodating many β-lactam substrates by having many of the catalytic residues on flexible loops, which explains the observed extended spectrum activity of this zinc dependent β-lactamase. Indeed, five loops contribute "keg" residues in the active site including side chains involved in metal binding. Loop 1 in particular, shows conformational flexibility, apparently related to the acceptance and positioning of substrates for cleavage by a zinc-activated water molecule. PubMed: 21931780DOI: 10.1371/journal.pone.0024621 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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