Structural highlights
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
Antibiotic resistance in bacterial pathogens poses a serious threat to human health and the metallo-beta-lactamase (MBL) enzymes are responsible for much of this resistance. The recently identified New Delhi MBL 1 (NDM-1) is a novel member of this family that is capable of hydrolysing a wide variety of clinically important antibiotics. Here, the crystal structure of NDM-1 from Klebsiella pneumoniae is reported and its structure and active site are discussed in the context of other recently deposited coordinates of NDM-1.
Structure of New Delhi metallo-beta-lactamase 1 (NDM-1).,Green VL, Verma A, Owens RJ, Phillips SE, Carr SB Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt, 10):1160-4. Epub 2011 Sep 6. PMID:22102018[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Green VL, Verma A, Owens RJ, Phillips SE, Carr SB. Structure of New Delhi metallo-beta-lactamase 1 (NDM-1). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt, 10):1160-4. Epub 2011 Sep 6. PMID:22102018 doi:10.1107/S1744309111029654
