Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 67, Issue -, Pages 1160-1164Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111029654
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Funding
- Medical Research Council
- MRC [MC_EX_G0901251, G0701506] Funding Source: UKRI
- Medical Research Council [MC_EX_G0901251, G0701506] Funding Source: researchfish
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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.
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