Solution structure of the strawberry allergen Fra a 1.
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.
Lehrstuhl Biopolymere und Forschungszentrum für Bio-Makromoleküle, Universität Bayreuth, Bayreuth, Germany.
Christian
C
Seutter von Loetzen
Kristian
K
Schweimer
Wilfried
W
Schwab
Paul
P
Rösch
Olivia
O
Hartl-Spiegelhauer
D052179:Antigens, Plant / Q000737:chemistry*; D002850:Chromatography, Gel; D002942:Circular Dichroism; D031985:Fragaria / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation
D052179:Antigens, Plant; C517508:Fra a 1 allergen, Fragaria ananassa; D010940:Plant Proteins