2RU4

Designed Armadillo Repeat Protein Self-ASsembled Complex (YIIM2-MAII)

2RU4 の概要

• エントリーDOI: 10.2210/pdb2ru4/pdb
• 関連するPDBエントリー: 2RU5
• NMR情報: BMRB: 11544
• 分子名称: Armadillo Repeat Protein, N-terminal fragment, YIIM2, Armadillo Repeat Protein, C-terminal fragment, MAII (2 entities in total)
• 機能のキーワード: solenoid repeat, armadillo repeat motif, de novo protein, self-assembly, solution complex
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21297.59

構造登録者

Zerbe, O.,Christen, M.T.,Plueckthun, A.,Watson, R.P. (登録日: 2013-11-22, 公開日: 2014-07-23, 最終更新日: 2024-05-15)

主引用文献

Watson, R.P.,Christen, M.T.,Ewald, C.,Bumbak, F.,Reichen, C.,Mihajlovic, M.,Schmidt, E.,Guntert, P.,Caflisch, A.,Pluckthun, A.,Zerbe, O.
Spontaneous self-assembly of engineered armadillo repeat protein fragments into a folded structure
Structure, 22:985-995, 2014

PubMed Abstract: Repeat proteins are built of modules, each of which constitutes a structural motif. We have investigated whether fragments of a designed consensus armadillo repeat protein (ArmRP) recognize each other. We examined a split ArmRP consisting of an N-capping repeat (denoted Y), three internal repeats (M), and a C-capping repeat (A). We demonstrate that the C-terminal MA fragment adopts a fold similar to the corresponding part of the entire protein. In contrast, the N-terminal YM2 fragment constitutes a molten globule. The two fragments form a 1:1 YM2:MA complex with a nanomolar dissociation constant essentially identical to the crystal structure of the continuous YM3A protein. Molecular dynamics simulations show that the complex is structurally stable over a 1 μs timescale and reveal the importance of hydrophobic contacts across the interface. We propose that the existence of a stable complex recapitulates possible intermediates in the early evolution of these repeat proteins.

PubMed: 24931467
DOI: 10.1016/j.str.2014.05.002

実験手法

SOLUTION NMR