Structural highlights
4eyb is a 2 chain structure with sequence from "bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 3q6x, 3spu, 4exs, 4exy, 4ey2, 4eyf, 4eyl |
| Gene: | blaNDM-1 ("Bacillus pneumoniae" (Schroeter 1886) Flugge 1886) |
| Activity: | Beta-lactamase, with EC number 3.5.2.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[BLAN1_KLEPN] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
Publication Abstract from PubMed
The beta-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-beta-lactamase-1 (NDM-1) has been found to confer enteric bacteria resistance to nearly all beta-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-beta-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 A, respectively, and represent the highest-resolution structural data for any metallo-beta-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-beta-lactamases.
New Delhi Metallo-beta-Lactamase: Structural Insights into beta-Lactam Recognition and Inhibition.,King DT, Worrall LJ, Gruninger R, Strynadka NC J Am Chem Soc. 2012 Jul 18;134(28):11362-5. Epub 2012 Jul 5. PMID:22713171[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ King DT, Worrall LJ, Gruninger R, Strynadka NC. New Delhi Metallo-beta-Lactamase: Structural Insights into beta-Lactam Recognition and Inhibition. J Am Chem Soc. 2012 Jul 18;134(28):11362-5. Epub 2012 Jul 5. PMID:22713171 doi:10.1021/ja303579d
