ArticleThe Journal of biological chemistry2014
Solution NMR structures of Pyrenophora tritici-repentis ToxB and its inactive homolog reveal potential determinants of toxin activity.
Article in The Journal of biological chemistry, 2014. 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.
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Computational studies reveal structural characterization and novel families of Puccinia striiformis f. sp. tritici effectors.PLoS computational biology · 2025Article
- Dual RNA-seq reveals distinct families of co-regulated and structurally conserved effectors in Botrytis cinerea infection of Arabidopsis thaliana.BMC biology · 2024Article
- The Molecular Docking of MAX Fungal Effectors with Plant HMA Domain-Binding Proteins.International journal of molecular sciences · 2023Article
- Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-TerminalMolecules (Basel, Switzerland) · 2023Article
- Ab Initio Modelling of the Structure of ToxA-like and MAX Fungal Effector Proteins.International journal of molecular sciences · 2023Article
- Article
- Remote homology clustering identifies lowly conserved families of effector proteins in plant-pathogenic fungi.Microbial genomics · 2021Article
- Deciphering the Infectious Process ofMicroorganisms · 2020Article
- Heterologous Expression of theFrontiers in microbiology · 2019Article
- Inverse gene-for-gene interactions contribute additively to tan spot susceptibility in wheat.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2017Article
- Effectors of Filamentous Plant Pathogens: Commonalities amid Diversity.Microbiology and molecular biology reviews : MMBR · 2017Review
- Recognition of theThe Plant cell · 2017Article
- Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds.Microbial cell factories · 2016Article
- Solution structure of an avirulence protein, AVR-Pia, from Magnaporthe oryzae.Journal of biomolecular NMR · 2015Article
- Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi.PLoS pathogens · 2015Article
- Residue-level global and local ensemble-ensemble comparisons of protein domains.Protein science : a publication of the Protein Society · 2015Article
- Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor.eLife · 2015Article
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8 authors.
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Abstract
Pyrenophora tritici-repentis Ptr ToxB (ToxB) is a proteinaceous host-selective toxin produced by Pyrenophora tritici-repentis (P. tritici-repentis), a plant pathogenic fungus that causes the disease tan spot of wheat. One feature that distinguishes ToxB from other host-selective toxins is that it has naturally occurring homologs in non-pathogenic P. tritici-repentis isolates that lack toxic activity. There are no high-resolution structures for any of the ToxB homologs, or for any protein with >30% sequence identity, and therefore what underlies activity remains an open question. Here, we present the NMR structures of ToxB and its inactive homolog Ptr toxb. Both proteins adopt a β-sandwich fold comprising three strands in each half that are bridged together by two disulfide bonds. The inactive toxb, however, shows higher flexibility localized to the sequence-divergent β-sandwich half. The absence of toxic activity is attributed to a more open structure in the vicinity of one disulfide bond, higher flexibility, and residue differences in an exposed loop that likely impacts interaction with putative targets. We propose that activity is regulated by perturbations in a putative active site loop and changes in dynamics distant from the site of activity. Interestingly, the new structures identify AvrPiz-t, a secreted avirulence protein produced by the rice blast fungus, as a structural homolog to ToxB. This homology suggests that fungal proteins involved in either disease susceptibility such as ToxB or resistance such as AvrPiz-t may have a common evolutionary origin.
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