ArticleThe Journal of biological chemistry2012
The 1.8 Å cholix toxin crystal structure in complex with NAD+ and evidence for a new kinetic model.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Discovery of mono-ADP ribosylating toxins with high structural homology to Pseudomonas exotoxin A.Communications biology · 2025Article
- GRP75 as a functional element of cholix transcytosis.Tissue barriers · 2023Article
- A Structural Approach to Anti-Virulence: A Discovery Pipeline.Microorganisms · 2021Article
- Review
- Cell Death Signaling Pathway Induced by Cholix Toxin, a Cytotoxin and eEF2 ADP-Ribosyltransferase Produced byToxins · 2020Review
- Crystal Structure of Exotoxin A fromToxins · 2020Article
- Cholix protein domain I functions as a carrier element for efficient apical to basal epithelial transcytosis.Tissue barriers · 2020Article
- Emissive Synthetic Cofactors: A Highly Responsive NADChemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Ligand Selectivity between the ADP-Ribosylating Toxins: An Inverse-Docking Study for Multitarget Drug Discovery.ACS omega · 2017Article
- The Father, Son and Cholix Toxin: The Third Member of the DT Group Mono-ADP-Ribosyltransferase Toxin Family.Toxins · 2015Review
- C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae.The Journal of biological chemistry · 2015Article
- Novel bacterial ADP-ribosylating toxins: structure and function.Nature reviews. Microbiology · 2014Review
- Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.Molecular aspects of medicine · 2013Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
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 Å 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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.