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Solution structure of the strawberry allergen Fra a 1.

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 ?-sheet, two short V-shaped ?-helices and a long C-terminal ?-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.

SUBMITTER: Seutter von Loetzen C

PROVIDER: S-EPMC3497729 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Solution structure of the strawberry allergen Fra a 1.

Seutter von Loetzen Christian C Schweimer Kristian K Schwab Wilfried W Rösch Paul P Hartl-Spiegelhauer Olivia O

Bioscience reports 20121201 6

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 ...[more]

PMID: 22913709

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