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Structure of New Delhi metallo-β-lactamase 1 (NDM-1).

DOI: 10.1107/S1744309111029654 DOI Help
PMID: 22102018 PMID Help

Authors: Victoria Green (Rutherford Appleton Laboratory, U.K.) , Anil Verma (Rutherford Appleton Laboratory, U.K.) , Raymond J Owens (Rutherford Appleton Laboratory, U.K.) , Simon E V Phillips (Rutherford Appleton Laboratory, U.K.) , Stephen B Carr (Rutherford Appleton Laboratory, U.K.)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology and Crystallization Communications , VOL 67 (10) , PAGES 1160-1164

State: Published (Approved)
Published: December 2011

Abstract: Antibiotic resistance in bacterial pathogens poses a serious threat to human health and the metallo--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.

Journal Keywords: Crystallography ; X-Ray ; Klebsiella; Models ; Molecular ; Protein; Tertiary ; beta-Lactamases

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

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