Solution structure of the strawberry allergen Fra a 1. Issue 6 (5th October 2012)

• Record Type: Journal Article
• Authors: Seutter von Loetzen, Christian; Schweimer, Kristian; Schwab, Wilfried; Rösch, Paul; Hartl-Spiegelhauer, Olivia
• Is Part Of: Bioscience reports. Volume 32:Issue 6(2012)
• Page Start: 567
• Page End: 575
• Publication Date: 2012-10-05
• Subjects: Bet v 1 superfamily -- Fra a 1 -- Fragaria x ananassa -- NMR structure -- pathogenesis-related protein; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1042/BSR20120058
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract : The PR10 family protein Fra a 1E from strawberry ( Fragaria x ananassa ) is down-regulated in white strawberry mutants, and transient RNAi (RNA interference)-mediated silencing experiments confirmed that Fra a 1 is involved in fruit pigment synthesis. In the present study, we determined the solution structure of Fra a 1E. The protein fold is identical with that of other members of the PR10 protein family and consists of a seven-stranded antiparallel β-sheet, two short V-shaped α-helices and a long C-terminal α-helix that encompass a hydrophobic pocket. Whereas Fra a 1E contains the glycine-rich loop that is highly conserved throughout the protein family, the volume of the hydrophobic pocket and the size of its entrance are much larger than expected. The three-dimensional structure may shed some light on its physiological function and may help to further understand the role of PR10 proteins in plants.