ArticleThe Journal of biological chemistry2010
Kinetic and structural insights into the mechanism of AMPylation by VopS Fic domain.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 91 citations in OpenAlex.
- The rise of AMPylation: from bacterial beginnings to modern implications in health and disease.Biochemical Society transactions · 2025Review
- Structural Insights into the Regulatory Mechanisms of the Toxic Activity of Sofic in Anti-Phage Defense Systems.International journal of molecular sciences · 2025Article
- Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025Review
- Article
- Cryo-EM Detection of AMPylated Histidine Implies Covalent Catalysis in AMPylation Mediated by a Bacterial Effector.Journal of molecular biology · 2025Article
- The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3.Communications biology · 2023Article
- Comparative genomics uncovered differences between clinical and environmental populations ofMicrobial genomics · 2023Article
- AMPylation and Endoplasmic Reticulum Protein Folding Homeostasis.Cold Spring Harbor perspectives in biology · 2023Review
- AMPylation of small GTPases by Fic enzymes.FEBS letters · 2023Review
- Catalytic deAMPylation in AMPylation-inhibitory/assistant forms of FICD protein.Frontiers in chemistry · 2023Article
- A secreted effector with a dual role as a toxin and as a transcriptional factor.Nature communications · 2022Article
- Analysis of the Type 4 Effectome across the GenusInternational journal of molecular sciences · 2022Article
- Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens.Veterinary research · 2021Review
- Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.Nature communications · 2021Article
- Investigation of the Detailed AMPylated Reaction Mechanism for the Huntingtin Yeast-Interacting Protein E Enzyme HYPE.International journal of molecular sciences · 2021Article
- Fic and non-Fic AMPylases: protein AMPylation in metazoans.Open biology · 2021Article
- Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD.Nature communications · 2021Article
- Structural basis for selective AMPylation of Rac-subfamily GTPases byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Adaptations ofFrontiers in microbiology · 2021Review
- Conserved residue His-257 ofThe Journal of biological chemistry · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The bacterial pathogen Vibrio parahemeolyticus manipulates host signaling pathways during infections by injecting type III effectors into the cytoplasm of the target cell. One of these effectors, VopS, blocks actin assembly by AMPylation of a conserved threonine residue in the switch 1 region of Rho GTPases. The modified GTPases are no longer able to interact with downstream effectors due to steric hindrance by the covalently linked AMP moiety. Herein we analyze the structure of VopS and its evolutionarily conserved catalytic residues. Steady-state analysis of VopS mutants provides kinetic understanding on the functional role of each residue for AMPylation activity by the Fic domain. Further mechanistic analysis of VopS with its two substrates, ATP and Cdc42, demonstrates that VopS utilizes a sequential mechanism to AMPylate Rho GTPases. Discovery of a ternary reaction mechanism along with structural insight provides critical groundwork for future studies for the family of AMPylators that modify hydroxyl-containing residues with AMP.
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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.