5JYS

Pry1 CAP domain

Summary for 5JYS

• Entry DOI: 10.2210/pdb5jys/pdb
• Related: 5ETE
• Descriptor: Protein PRY1, MAGNESIUM ION (3 entities in total)
• Functional Keywords: cap protein, transport protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Cellular location: Secreted : P47032
• Total number of polymer chains: 1
• Total formula weight: 30544.16

Authors

Asojo, O.A. (deposition date: 2016-05-15, release date: 2016-07-20, Last modification date: 2024-11-06)

Primary citation

Darwiche, R.,Kelleher, A.,Hudspeth, E.M.,Schneiter, R.,Asojo, O.A.
Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) protein.
Sci Rep, 6:28838-28838, 2016

PubMed 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.

PubMed: 27344972
DOI: 10.1038/srep28838

Experimental method

X-RAY DIFFRACTION (1.901 Å)