ArticleNature communications2021
Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Reprogramming of bacterial virulence by lysine acetylation.Nature communications · 2026Article
- XopA: a novel type III secretion system effector inMicrobiology spectrum · 2026Article
- A bacterial YopJ-family acetyltransferase suppresses host immune response by Nε-acetylation of JAK1.Nature communications · 2026Article
- The Recognition of YopJ Family Effectors Depends on ZAR1/JIM2 Immune Complex in Nicotiana benthamiana.Molecular plant pathology · 2026Article
- A dramatic protein fold switch powers a bactericidal nanomachine.bioRxiv : the preprint server for biology · 2026Article
- Article
- Interaction of Potato Autophagy-Related StATG8 Family Proteins with Pathogen Effector and WRKY Transcription Factor in the Nucleus.Microorganisms · 2025Article
- Large-scale predictions of alternative protein conformations by AlphaFold2-based sequence association.Nature communications · 2025Article
- Molecular Dialog ofInternational journal of molecular sciences · 2025Review
- APlants (Basel, Switzerland) · 2025Article
- Optimization ultrasonic-assisted aqueous two-phase extraction of glabridin from licorice root and its activity against the foodborne pathogen MRSA.Food chemistry: X · 2025Article
- AlphaFold predictions of fold-switched conformations are driven by structure memorization.Nature communications · 2024Article
- Investigating the impact of insertion sequences and transposons in the genomes of the most significant phytopathogenic bacteria.Microbial genomics · 2024Article
- Article
- Evolutionary selection of proteins with two folds.Nature communications · 2023Article
- Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Molecular basis of ligand selectivity for melatonin receptors.RSC advances · 2023Article
- From prediction to function: Current practices and challenges towards the functional characterization of type III effectors.Frontiers in microbiology · 2023Review
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Yersinia outer protein J (YopJ) family effectors are widely deployed through the type III secretion system by both plant and animal pathogens. As non-canonical acetyltransferases, the enzymatic activities of YopJ family effectors are allosterically activated by the eukaryote-specific ligand inositol hexaphosphate (InsP6). However, the underpinning molecular mechanism remains undefined. Here we present the crystal structure of apo-PopP2, a YopJ family member secreted by the plant pathogen Ralstonia solanacearum. Structural comparison of apo-PopP2 with the InsP6-bound PopP2 reveals a substantial conformational readjustment centered in the substrate-binding site. Combining biochemical and computational analyses, we further identify a mechanism by which the association of InsP6 with PopP2 induces an α-helix-to-β-strand transition in the catalytic core, resulting in stabilization of the substrate recognition helix in the target protein binding site. Together, our study uncovers the molecular basis governing InsP6-mediated allosteric regulation of YopJ family acetyltransferases and further expands the paradigm of fold-switching proteins.
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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 Socratic graph.