2BRZ

SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN BRAZZEIN, MINIMIZED AVERAGE STRUCTURE

2BRZ の概要

• エントリーDOI: 10.2210/pdb2brz/pdb
• 分子名称: BRAZZEIN (1 entity in total)
• 機能のキーワード: sweet protein, cysteine-stabilized alpha-beta
• 由来する生物種: Pentadiplandra brazzeana
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6491.33

構造登録者

Caldwell, J.E.,Abildgaard, F.,Dzakula, Z.,Ming, D.,Hellekant, G.,Markley, J.L. (登録日: 1998-04-30, 公開日: 1998-07-01, 最終更新日: 2019-12-25)

主引用文献

Caldwell, J.E.,Abildgaard, F.,Dzakula, Z.,Ming, D.,Hellekant, G.,Markley, J.L.
Solution structure of the thermostable sweet-tasting protein brazzein.
Nat.Struct.Biol., 5:427-431, 1998

PubMed Abstract: The fruit of Pentadiplandra brazzeana Baillon contains a small, sweet-tasting protein named brazzein. The structure of brazzein in solution was determined by proton nuclear magnetic resonance spectroscopy at pH 5.2 and 22 degrees C. The brazzein fold, which contains one alpha-helix and three strands of antiparallel beta-sheet, does not resemble that of either of the other two sweet-tasting proteins with known structures, monellin and thaumatin. Instead, the structure of brazzein resembles those of plant gamma-thionins and defensins and arthropod toxins. Sequence comparisons predict that members of a newly-identified family of serine proteinase inhibitors share the brazzein fold.

PubMed: 9628478
DOI: 10.1038/nsb0698-427

実験手法

SOLUTION NMR