ArticleThe Plant cell2009
Crystal structure of the complex between Pseudomonas effector AvrPtoB and the tomato Pto kinase reveals both a shared and a unique interface compared with AvrPto-Pto.
Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 83 citations in OpenAlex.
- Structural and functional characterization of VapBC52 toxin-antitoxin system from Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Bioinformatics Analysis of the TomatoPlants (Basel, Switzerland) · 2025Article
- Pattern Recognition Receptors in Plant Immunity.Advances in experimental medicine and biology · 2025Review
- Structural and biochemical basis of Arabidopsis FERONIA receptor kinase-mediated early signaling initiation.Plant communications · 2023Article
- Article
- Pto Interaction Proteins: Critical Regulators in Plant Development and Stress Response.Frontiers in plant science · 2022Review
- α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.International journal of molecular sciences · 2021Review
- NOD-like receptor-mediated plant immunity: from structure to cell death.Nature reviews. Immunology · 2021Review
- Article
- A molecular roadmap to the plant immune system.The Journal of biological chemistry · 2020Review
- Molecular Characterization of Differences between the Tomato Immune Receptors Flagellin Sensing 3 and Flagellin Sensing 2.Plant physiology · 2020Article
- Perturbations of the ZED1 pseudokinase activate plant immunity.PLoS pathogens · 2019Article
- Identification and analysis of structurally critical fragments in HopS2.BMC bioinformatics · 2019Article
- Diverse mechanisms of resistance to Pseudomonas syringae in a thousand natural accessions of Arabidopsis thaliana.The New phytologist · 2017Article
- Behind the lines-actions of bacterial type III effector proteins in plant cells.FEMS microbiology reviews · 2016Review
- Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54.The Journal of biological chemistry · 2016Article
- Fine-mapping of a major QTL controlling angular leaf spot resistance in common bean (Phaseolus vulgaris L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2015Article
- The N-terminal domain of the tomato immune protein Prf contains multiple homotypic and Pto kinase interaction sites.The Journal of biological chemistry · 2015Article
- Perturbation of host ubiquitin systems by plant pathogen/pest effector proteins.Cellular microbiology · 2015Review
- Repeat-containing protein effectors of plant-associated organisms.Frontiers in plant science · 2015Review
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7 authors at 5 institutions in 2 countries.
Funding
Abstract
Resistance to bacterial speck disease in tomato (Solanum lycopersicum) is activated upon recognition by the host Pto kinase of either one of two sequence-unrelated effector proteins, AvrPto or AvrPtoB, from Pseudomonas syringae pv tomato (Pst). Pto induces Pst immunity by acting in concert with the Prf protein. The recently reported structure of the AvrPto-Pto complex revealed that interaction of AvrPto with Pto appears to relieve an inhibitory effect of Pto, allowing Pto to activate Prf. Here, we present the crystal structure of the Pto binding domain of AvrPtoB (residues 121 to 205) at a resolution of 1.9A and of the AvrPtoB(121-205)-Pto complex at a resolution of 3.3 A. AvrPtoB(121-205) exhibits a tertiary fold that is completely different from that of AvrPto, and its conformation remains largely unchanged upon binding to Pto. In common with AvrPto-Pto, the AvrPtoB-Pto complex relies on two interfaces. One of these interfaces is similar in both complexes, although the primary amino acid sequences from the two effector proteins are very different. Amino acid substitutions in Pto at the other interface disrupt the interaction of AvrPtoB-Pto but not that of AvrPto-Pto. Interestingly, substitutions in Pto affecting this unique interface also cause Pto to induce Prf-dependent host cell death independently of either effector protein.
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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 OpenQuestion graph.