ArticleScientific reports2016
Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) protein.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Foliar Pine Pathogens From Different Kingdoms Share Defence-Eliciting Effector Proteins.Molecular plant pathology · 2025Article
- The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.Genetics · 2025Article
- CAP superfamily proteins (VdPRYs) manipulate plant immunity and contribute to the virulence ofMycology · 2025Article
- Dual functionality of pathogenesis-related proteins: defensive role in plants versus immunosuppressive role in pathogens.Frontiers in plant science · 2024Article
- Article
- The function of plant PR1 and other members of the CAP protein superfamily in plant-pathogen interactions.Molecular plant pathology · 2023Review
- Human lipocalins bind and export fatty acids through the secretory pathway of yeast cells.Frontiers in microbiology · 2023Article
- Plasmodium falciparum Cysteine Rich Secretory Protein uniquely localizes to one end of male gametes.Molecular and biochemical parasitology · 2022Article
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
- The yeast cell wall protein Pry3 inhibits mating through highly conserved residues within the CAP domain.Biology open · 2020Article
- Conserved nuclear hormone receptors controlling a novel plastic trait target fast-evolving genes expressed in a single cell.PLoS genetics · 2020Article
- Article
- Metal ions and redox balance regulate distinct amyloid-like aggregation pathways of GAPR-1.Scientific reports · 2019Article
- Zinc binding regulates amyloid-like aggregation of GAPR-1.Bioscience reports · 2019Article
- Crystal structure of Brugia malayi venom allergen-like protein-1 (BmVAL-1), a vaccine candidate for lymphatic filariasis.International journal for parasitology · 2018Article
- Heligmosomoides polygyrus Venom Allergen-like Protein-4 (HpVAL-4) is a sterol binding protein.International journal for parasitology · 2018Article
- Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans.PloS one · 2018Article
- Plant pathogenesis-related proteins of the cacao fungal pathogenThe Journal of biological chemistry · 2017Article
- Structural insights into the interaction of the conserved mammalian proteins GAPR-1 and Beclin 1, a key autophagy protein.Acta crystallographica. Section D, Structural biology · 2017Article
- Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches' Broom Disease of Cacao.Scientific reports · 2017Article
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5 authors.
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Abstract
The production, crystal structure, and functional characterization of the C-terminal cysteine-rich secretory protein/antigen 5/pathogenesis related-1 (CAP) domain of pathogen-related yeast protein-1 (Pry1) from Saccharomyces cerevisiae is presented. The CAP domain of Pry1 (Pry1CAP) is functional in vivo as its expression restores cholesterol export to yeast mutants lacking endogenous Pry1 and Pry2. Recombinant Pry1CAP forms dimers in solution, is sufficient for in vitro cholesterol binding, and has comparable binding properties as full-length Pry1. Two crystal structures of Pry1CAP are reported, one with Mg(2+) coordinated to the conserved CAP tetrad (His208, Glu215, Glu233 and His250) in spacegroup I41 and the other without divalent cations in spacegroup P6122. The latter structure contains four 1,4-dioxane molecules from the crystallization solution, one of which sits in the cholesterol binding site. Both structures reveal that the divalent cation and cholesterol binding sites are connected upon dimerization, providing a structural basis for the observed Mg(2+)-dependent sterol binding by Pry1.
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