2LPX
Solution Structure of Strawberry Allergen Fra a 1e
Summary for 2LPX
| Entry DOI | 10.2210/pdb2lpx/pdb |
| NMR Information | BMRB: 18281 |
| Descriptor | Major strawberry allergen Fra a 1-E (1 entity in total) |
| Functional Keywords | bet v 1 homologous protein, unknown function |
| Biological source | Fragaria x ananassa (strawberry) |
| Total number of polymer chains | 1 |
| Total formula weight | 19012.43 |
| Authors | Seutter von Loetzen, C.,Hartl-Spiegelhauer, O.,Schweimer, K.,Schwab, W.,Roesch, P. (deposition date: 2012-02-20, release date: 2012-03-07, Last modification date: 2024-05-15) |
| Primary citation | Seutter von Loetzen, C.,Schweimer, K.,Schwab, W.,Rosch, P.,Hartl-Spiegelhauer, O. Solution structure of the strawberry allergen Fra a 1. Biosci.Rep., 32:567-575, 2012 Cited by PubMed 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. PubMed: 22913709DOI: 10.1042/BSR20120058 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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