ArticleProceedings of the National Academy of Sciences of the United States of America2013
Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 48 papers.
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48 citing papers in PubMed.
- Development and Validation of a High-Throughput Screening Assay for the Legionella ADP-Ribosyl Transferase SdeA.Chembiochem : a European journal of chemical biology · 2025Article
- Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli.Nature communications · 2025Article
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
- General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase-Substrate Complexes.Toxins · 2024Review
- Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs.Nature chemical biology · 2024Article
- An Updated View on the Cellular Uptake and Mode-of-Action of Clostridioides difficile Toxins.Advances in experimental medicine and biology · 2024Article
- Cellular Uptake and Cytotoxicity ofToxins · 2023Review
- Regulation of Biomolecular Condensates by Poly(ADP-ribose).Chemical reviews · 2023Review
- Novel secreted STPKLRR from Vibrio splendidus AJ01 promotes pathogen internalization via mediating tropomodulin phosphorylation dependent cytoskeleton rearrangement.PLoS pathogens · 2023Article
- Structural mechanisms of calmodulin activation of Shigella effector OspC3 to ADP-riboxanate caspase-4/11 and block pyroptosis.Nature structural & molecular biology · 2023Article
- Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin.Nature communications · 2022Article
- Crystal structures of pertussis toxin with NADThe Journal of biological chemistry · 2022Article
- The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis.The Journal of biological chemistry · 2021Review
- Enhanced Molecular Dynamics Method to Efficiently Increase the Discrimination Capability of Computational Protein-Protein Docking.Journal of chemical theory and computation · 2021Article
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- On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits.International journal of molecular sciences · 2021Review
- Crystal structure of bacterial cytotoxic necrotizing factor CNFThe EMBO journal · 2021Article
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- Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases.Toxins · 2021Review
Corrections and comments
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- Erratum issued
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium perfringens iota-toxin (Ia) mono-ADP ribosylates Arg177 of actin, leading to cytoskeletal disorganization and cell death. To fully understand the reaction mechanism of arginine-specific mono-ADP ribosyl transferase, the structure of the toxin-substrate protein complex must be characterized. Recently, we solved the crystal structure of Ia in complex with actin and the nonhydrolyzable NAD(+) analog βTAD (thiazole-4-carboxamide adenine dinucleotide); however, the structures of the NAD(+)-bound form (NAD(+)-Ia-actin) and the ADP ribosylated form [Ia-ADP ribosylated (ADPR)-actin] remain unclear. Accidentally, we found that ethylene glycol as cryo-protectant inhibits ADP ribosylation and crystallized the NAD(+)-Ia-actin complex. Here we report high-resolution structures of NAD(+)-Ia-actin and Ia-ADPR-actin obtained by soaking apo-Ia-actin crystal with NAD(+) under different conditions. The structures of NAD(+)-Ia-actin and Ia-ADPR-actin represent the pre- and postreaction states, respectively. By assigning the βTAD-Ia-actin structure to the transition state, the strain-alleviation model of ADP ribosylation, which we proposed previously, is experimentally confirmed and improved. Moreover, this reaction mechanism appears to be applicable not only to Ia but also to other ADP ribosyltransferases.
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