期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 287, 期 25, 页码 21176-21188出版社
ELSEVIER
DOI: 10.1074/jbc.M111.337311
关键词
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资金
- Natural Sciences and Engineering Research Council
- Canadian Institutes of Health Research
- Cystic Fibrosis Canada
- Canadian Institutes of Health Research, Cystic Fibrosis Canada
- Human Frontier Science Program
- Carlsberg-fondet
Certain Vibrio cholerae strains produce cholix, a potent protein toxin that has diphthamide-specific ADP-ribosyltransferase activity against eukaryotic elongation factor 2. Here we present a 1.8 angstrom crystal structure of cholix in complex with its natural substrate, nicotinamide adenine dinucleotide (NAD(+)). We also substituted hallmark catalytic residues by site-directed mutagenesis and analyzed both NAD(+) binding and ADP-ribosyltransferase activity using a fluorescence-based assay. These data are the basis for a new kinetic model of cholix toxin activity. Further, the new structural data serve as a reference for continuing inhibitor development for this toxin class.
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