2LY5

Refined solution structure of recombinant brazzein

2LY5 の概要

• エントリーDOI: 10.2210/pdb2ly5/pdb
• 関連するPDBエントリー: 2LY6
• NMR情報: BMRB: 16215
• 分子名称: Defensin-like protein (1 entity in total)
• 機能のキーワード: cys-sail, rdc, brazzein, plant protein
• 由来する生物種: Pentadiplandra brazzeana
• 細胞内の位置: Secreted: P56552
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6380.23

構造登録者

Cornilescu, C.C.,Cornilescu, G.,Tonelli, M.,Markley, J.L.,Assadi-Porter, F.M. (登録日: 2012-09-12, 公開日: 2013-01-30, 最終更新日: 2024-11-27)

主引用文献

Cornilescu, C.C.,Cornilescu, G.,Rao, H.,Porter, S.F.,Tonelli, M.,Derider, M.L.,Markley, J.L.,Assadi-Porter, F.M.
Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein.
Proteins, 81:919-925, 2013

PubMed Abstract: The sweet protein brazzein, a member of the Csβα fold family, contains four disulfide bonds that lend a high degree of thermal and pH stability to its structure. Nevertheless, a variable temperature study has revealed that the protein undergoes a local, reversible conformational change between 37 and 3°C with a midpoint about 27°C that changes the orientations and side-chain hydrogen bond partners of Tyr8 and Tyr11. To test the functional significance of this effect, we used NMR saturation transfer to investigate the interaction between brazzein and the amino terminal domain of the sweet receptor subunit T1R2; the results showed a stronger interaction at 7°C than at 37°C. Thus the low temperature conformation, which alters the orientations of two loops known to be critical for the sweetness of brazzein, may represent the bound state of brazzein in the complex with the human sweet receptor.

PubMed: 23349025
DOI: 10.1002/prot.24259

実験手法

SOLUTION NMR