2LPX

Solution Structure of Strawberry Allergen Fra a 1e

2LPX の概要

• エントリーDOI: 10.2210/pdb2lpx/pdb
• NMR情報: BMRB: 18281
• 分子名称: Major strawberry allergen Fra a 1-E (1 entity in total)
• 機能のキーワード: bet v 1 homologous protein, unknown function
• 由来する生物種: Fragaria x ananassa (strawberry)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19012.43

構造登録者

Seutter von Loetzen, C.,Hartl-Spiegelhauer, O.,Schweimer, K.,Schwab, W.,Roesch, P. (登録日: 2012-02-20, 公開日: 2012-03-07, 最終更新日: 2024-05-15)

主引用文献

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

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: 22913709
DOI: 10.1042/BSR20120058

実験手法

SOLUTION NMR