ArticleProceedings of the National Academy of Sciences of the United States of America2001
Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. 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, 154 citations in OpenAlex.
- Revisiting interactions between polygalacturonases and polygalacturonase-inhibiting proteins and their effects on plant health: a review.Frontiers in plant science · 2025Review
- Genetic and Functional Diversity Help Explain Pathogenic, Weakly Pathogenic, and Commensal Lifestyles in the Genus Xanthomonas.Genome biology and evolution · 2024Article
- Plant polygalacturonase structures specify enzyme dynamics and processivities to fine-tune cell wall pectins.The Plant cell · 2023Article
- Laccaria bicolor pectin methylesterases are involved in ectomycorrhiza development with Populus tremula × Populus tremuloides.The New phytologist · 2022Article
- The Identification and Characterization of Endopolygalacturonases in a South African Isolate ofMicroorganisms · 2022Article
- Functional Classification and Characterization of the Fungal Glycoside Hydrolase 28 Protein Family.Journal of fungi (Basel, Switzerland) · 2022Article
- Transcriptional Basis for Haustorium Formation and Host Establishment in HemiparasiticFrontiers in genetics · 2022Article
- Gibberellin-regulated proteins: Emergent allergens.Frontiers in allergy · 2022Article
- Exploring the potential of engineering polygalacturonase-inhibiting protein as an ecological, friendly, and nontoxic pest control agent.Biotechnology and bioengineering · 2021Article
- Comprehensive Leaf Cell Wall Analysis Using Carbohydrate Microarrays Reveals Polysaccharide-Level Variation betweenPolymers · 2021Article
- Article
- Industrial Use of Cell Wall Degrading Enzymes: The Fine Line Between Production Strategy and Economic Feasibility.Frontiers in bioengineering and biotechnology · 2020Review
- Crystal structure of the catalytic unit of GH 87-type α-1,3-glucanase Agl-KA from Bacillus circulans.Scientific reports · 2019Article
- Amino acid substitutions in a polygalacturonase inhibiting protein (OsPGIP2) increases sheath blight resistance in rice.Rice (New York, N.Y.) · 2019Article
- High-level secretive expression of a novel achieved Talaromyces cellulolyticus endo-polygalacturonase in Pichia pastoris by improving gene dosage for hydrolysis of natural pectin.World journal of microbiology & biotechnology · 2019Article
- Pectinase secreted by psychrotolerant fungi: identification, molecular characterization and heterologous expression of a cold-active polygalacturonase from Tetracladium sp.Microbial cell factories · 2019Article
- Evolutionary Analysis of Pectin Lyases of the Genus Colletotrichum.Journal of molecular evolution · 2017Article
- Article
- Genomic characterization of plant cell wall degrading enzymes and in silico analysis of xylanases and polygalacturonases of Fusarium virguliforme.BMC microbiology · 2016Article
- A phage display-selected peptide inhibitor of Agrobacterium vitis polygalacturonase.Molecular plant pathology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To invade a plant tissue, phytopathogenic fungi produce several cell wall-degrading enzymes; among them, endopolygalacturonase (PG) catalyzes the fragmentation and solubilization of homogalacturonan. Polygalacturonase-inhibiting proteins (PGIPs), found in the cell wall of many plants, counteract fungal PGs by forming specific complexes with them. We report the crystal structure at 1.73 A resolution of PG from the phytopathogenic fungus Fusarium moniliforme (FmPG). The structure of FmPG was useful to study the mode of interaction of the enzyme with PGIP-2 from Phaseolus vulgaris. Several amino acids of FmPG were mutated, and their contribution to the formation of the complex with PGIP-2 was investigated by surface plasmon resonance. The residues Lys-269 and Arg-267, located inside the active site cleft, and His-188, at the edge of the active site cleft, are critical for the formation of the complex, which is consistent with the observed competitive inhibition of the enzyme played by PGIP-2. The replacement of His-188 with a proline or the insertion of a tryptophan after position 270, variations that both occur in plant PGs, interferes with the formation of the complex. We suggest that these variations are important structural requirements of plant PGs to prevent PGIP binding.
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