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3s0z

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3s0z, resolution 2.50Å ()
Ligands:
Gene: blaNDM-1 (Escherichia coli)


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Crystal structure of New Delhi Metallo-beta-lactamase (NDM-1)

Publication Abstract from PubMed

Gram-negative Enterobacteriaceae with resistance to carbapenem conferred by New Delhi metallo-beta-lactamase 1 (NDM-1) are a type of newly discovered antibioticresistant bacteria. The rapid pandemic spread of NDM-1 bacteria worldwide (spreading to India, Pakistan, Europe, America, and Chinese Taiwan) in less than 2 months characterizes these microbes as a potentially major global health problem. The drug resistance of NDM-1 bacteria is largely due to plasmids containing the blaNDM-1 gene shuttling through bacterial populations. The NDM-1 enzyme encoded by the blaNDM-1 gene hydrolyzes beta-lactam antibiotics, allowing the bacteria to escape the action of antibiotics. Although the biological functions and structural features of NDM-1 have been proposed according to results from functional and structural investigation of its homologues, the precise molecular characteristics and mechanism of action of NDM-1 have not been clarified. Here, we report the three-dimensional structure of NDM-1 with two catalytic zinc ions in its active site. Biological and mass spectroscopy results revealed that D-captopril can effectively inhibit the enzymatic activity of NDM-1 by binding to its active site with high binding affinity. The unique features concerning the primary sequence and structural conformation of the active site distinguish NDM-1 from other reported metallo-beta-lactamases (MBLs) and implicate its role in wide spectrum drug resistance. We also discuss the molecular mechanism of NDM-1 action and its essential role in the pandemic of drug-resistant NDM-1 bacteria. Our results will provide helpful information for future drug discovery targeting drug resistance caused by NDM-1 and related metallo-beta-lactamases.

A structural view of the antibiotic degradation enzyme NDM-1 from a superbug., Guo Y, Wang J, Niu G, Shui W, Sun Y, Zhou H, Zhang Y, Yang C, Lou Z, Rao Z, Protein Cell. 2011 May;2(5):384-94. Epub 2011 Jun 2. PMID:21637961

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3s0z is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Guo Y, Wang J, Niu G, Shui W, Sun Y, Zhou H, Zhang Y, Yang C, Lou Z, Rao Z. A structural view of the antibiotic degradation enzyme NDM-1 from a superbug. Protein Cell. 2011 May;2(5):384-94. Epub 2011 Jun 2. PMID:21637961 doi:10.1007/s13238-011-1055-9

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