7A8S

de novo designed ba8-barrel sTIM11 with an alpha-helical extension

7A8S の概要

• エントリーDOI: 10.2210/pdb7a8s/pdb
• 関連するPDBエントリー: 5BVL 6YQY
• 分子名称: sTIM11_h3, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: protein design, tim-barrel, stim11, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23685.77

構造登録者

Shanmugaratnam, S.,Wiese, J.G.,Hocker, B. (登録日: 2020-08-31, 公開日: 2021-03-24, 最終更新日: 2024-01-31)

主引用文献

Wiese, J.G.,Shanmugaratnam, S.,Hocker, B.
Extension of a de novo TIM barrel with a rationally designed secondary structure element.
Protein Sci., 30:982-989, 2021

PubMed Abstract: The ability to construct novel enzymes is a major aim in de novo protein design. A popular enzyme fold for design attempts is the TIM barrel. This fold is a common topology for enzymes and can harbor many diverse reactions. The recent de novo design of a four-fold symmetric TIM barrel provides a well understood minimal scaffold for potential enzyme designs. Here we explore opportunities to extend and diversify this scaffold by adding a short de novo helix on top of the barrel. Due to the size of the protein, we developed a design pipeline based on computational ab initio folding that solves a less complex sub-problem focused around the helix and its vicinity and adapt it to the entire protein. We provide biochemical characterization and a high-resolution X-ray structure for one variant and compare it to our design model. The successful extension of this robust TIM-barrel scaffold opens opportunities to diversify it towards more pocket like arrangements and as such can be considered a building block for future design of binding or catalytic sites.

PubMed: 33723882
DOI: 10.1002/pro.4064

実験手法

X-RAY DIFFRACTION (1.58 Å)