2lpx
Solution Structure of Strawberry Allergen Fra a 1e
Structural highlights
FunctionFRA1E_FRAAN Involved in the control of flavonoid biosynthesis in fruits, probably by binding directly to natural flavonoids (PubMed:19969523). Binds the natural flavonoid quercetin-3-O-glucuronide with affinities in the low micromolar range (PubMed:24133217).[1] [2] Publication Abstract from PubMedThe 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 beta-sheet, two short V-shaped alpha-helices and a long C-terminal alpha-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. Solution structure of the strawberry allergen Fra a 1.,Seutter von Loetzen C, Schweimer K, Schwab W, Rosch P, Hartl-Spiegelhauer O Biosci Rep. 2012 Dec 1;32(6):567-75. doi: 10.1042/BSR20120058. PMID:22913709[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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