5EZC

A de novo designed heptameric coiled coil CC-Hept-I18C-L22H-I25E

5EZC の概要

• エントリーDOI: 10.2210/pdb5ezc/pdb
• 関連するPDBエントリー: 4pna
• 分子名称: CC-Hept-C-H-E (2 entities in total)
• 機能のキーワード: coiled coil, heptamer, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 23673.66

構造登録者

Burton, A.J.,Brady, R.L.,Woolfson, D.N. (登録日: 2015-11-26, 公開日: 2016-07-06, 最終更新日: 2024-11-20)

主引用文献

Burton, A.J.,Thomson, A.R.,Dawson, W.M.,Brady, R.L.,Woolfson, D.N.
Installing hydrolytic activity into a completely de novo protein framework.
Nat.Chem., 8:837-844, 2016

PubMed Abstract: The design of enzyme-like catalysts tests our understanding of sequence-to-structure/function relationships in proteins. Here we install hydrolytic activity predictably into a completely de novo and thermostable α-helical barrel, which comprises seven helices arranged around an accessible channel. We show that the lumen of the barrel accepts 21 mutations to functional polar residues. The resulting variant, which has cysteine-histidine-glutamic acid triads on each helix, hydrolyses p-nitrophenyl acetate with catalytic efficiencies that match the most-efficient redesigned hydrolases based on natural protein scaffolds. This is the first report of a functional catalytic triad engineered into a de novo protein framework. The flexibility of our system also allows the facile incorporation of unnatural side chains to improve activity and probe the catalytic mechanism. Such a predictable and robust construction of truly de novo biocatalysts holds promise for applications in chemical and biochemical synthesis.

PubMed: 27554410
DOI: 10.1038/nchem.2555

実験手法

X-RAY DIFFRACTION (1.8 Å)