3HOJ

Crystal Structure of a Novel Engineered Retroaldolase: RA-22

「3B5V」から置き換えられました

3HOJ の概要

• エントリーDOI: 10.2210/pdb3hoj/pdb
• 関連するPDBエントリー: 3B5L
• 分子名称: RETROALDOLASE-22 (2 entities in total)
• 機能のキーワード: tim barrel, retroaldolase, engineered computationally designed, lyase
• 由来する生物種: artificial gene
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28456.82

構造登録者

Stoddard, B.L.,Doyle, L.A. (登録日: 2009-06-02, 公開日: 2009-08-25, 最終更新日: 2024-02-21)

主引用文献

Jiang, L.,Althoff, E.A.,Clemente, F.R.,Doyle, L.,Rothlisberger, D.,Zanghellini, A.,Gallaher, J.L.,Betker, J.L.,Tanaka, F.,Barbas, C.F.,Hilvert, D.,Houk, K.N.,Stoddard, B.L.,Baker, D.
De Novo Computational Design of Retro-Aldol Enzymes
Science, 319:1387-1391, 2008

PubMed Abstract: The creation of enzymes capable of catalyzing any desired chemical reaction is a grand challenge for computational protein design. Using new algorithms that rely on hashing techniques to construct active sites for multistep reactions, we designed retro-aldolases that use four different catalytic motifs to catalyze the breaking of a carbon-carbon bond in a nonnatural substrate. Of the 72 designs that were experimentally characterized, 32, spanning a range of protein folds, had detectable retro-aldolase activity. Designs that used an explicit water molecule to mediate proton shuffling were significantly more successful, with rate accelerations of up to four orders of magnitude and multiple turnovers, than those involving charged side-chain networks. The atomic accuracy of the design process was confirmed by the x-ray crystal structure of active designs embedded in two protein scaffolds, both of which were nearly superimposable on the design model.

PubMed: 18323453
DOI: 10.1126/SCIENCE.1152692

実験手法

X-RAY DIFFRACTION (2.2 Å)