5ete Citations

Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) protein.

OpenAccess logo Sci Rep 6 28838 (2016)
Cited: 10 times
EuropePMC logo PMID: 27344972

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.

Reviews citing this publication (2)

  1. The function of yeast CAP family proteins in lipid export, mating, and pathogen defense. Darwiche R, El Atab O, Cottier S, Schneiter R. FEBS Lett. 592 1304-1311 (2018)
  2. Emerging Insights into the Functions of Pathogenesis-Related Protein 1. Breen S, Williams SJ, Outram M, Kobe B, Solomon PS. Trends Plant Sci. 22 871-879 (2017)

Articles citing this publication (8)

  1. The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein. Darwiche R, Mène-Saffrané L, Gfeller D, Asojo OA, Schneiter R. J. Biol. Chem. 292 8304-8314 (2017)
  2. Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches' Broom Disease of Cacao. Baroni RM, Luo Z, Darwiche R, Hudspeth EM, Schneiter R, Pereira GAG, Mondego JMC, Asojo OA. Sci Rep 7 7818 (2017)
  3. Plant pathogenesis-related proteins of the cacao fungal pathogen Moniliophthora perniciosa differ in their lipid-binding specificities. Darwiche R, El Atab O, Baroni RM, Teixeira PJPL, Mondego JMC, Pereira GAG, Schneiter R. J. Biol. Chem. 292 20558-20569 (2017)
  4. Zinc binding regulates amyloid-like aggregation of GAPR-1. Sheng J, Olrichs NK, Geerts WJ, Li X, Rehman AU, Gadella BM, Kaloyanova DV, Helms JB. Biosci. Rep. 39 (2019)
  5. Crystal structure of Brugia malayi venom allergen-like protein-1 (BmVAL-1), a vaccine candidate for lymphatic filariasis. Darwiche R, Lugo F, Drurey C, Varossieau K, Smant G, Wilbers RHP, Maizels RM, Schneiter R, Asojo OA. Int. J. Parasitol. 48 371-378 (2018)
  6. Heligmosomoides polygyrus Venom Allergen-like Protein-4 (HpVAL-4) is a sterol binding protein. Asojo OA, Darwiche R, Gebremedhin S, Smant G, Lozano-Torres JL, Drurey C, Pollet J, Maizels RM, Schneiter R, Wilbers RHP. Int. J. Parasitol. 48 359-369 (2018)
  7. Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans. Bantel Y, Darwiche R, Rupp S, Schneiter R, Sohn K. PLoS ONE 13 e0201932 (2018)
  8. Metal ions and redox balance regulate distinct amyloid-like aggregation pathways of GAPR-1. Sheng J, Olrichs NK, Geerts WJ, Kaloyanova DV, Helms JB. Sci Rep 9 15048 (2019)