7LDF

High resolution NMR solution structure of a de novo designed minimal thioredoxin fold protein

7LDF の概要

• エントリーDOI: 10.2210/pdb7ldf/pdb
• NMR情報: BMRB: 30844
• 分子名称: Minimal thioredoxin fold protein, ems_thioM_802 (1 entity in total)
• 機能のキーワード: de novo designed, 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: 8366.35

構造登録者

Urbauer, J.L.,Strauch, E.M. (登録日: 2021-01-13, 公開日: 2022-07-13, 最終更新日: 2024-05-15)

主引用文献

Linsky, T.W.,Noble, K.,Tobin, A.R.,Crow, R.,Carter, L.,Urbauer, J.L.,Baker, D.,Strauch, E.M.
Sampling of structure and sequence space of small protein folds.
Nat Commun, 13:7151-7151, 2022

PubMed Abstract: Nature only samples a small fraction of the sequence space that can fold into stable proteins. Furthermore, small structural variations in a single fold, sometimes only a few amino acids, can define a protein's molecular function. Hence, to design proteins with novel functionalities, such as molecular recognition, methods to control and sample shape diversity are necessary. To explore this space, we developed and experimentally validated a computational platform that can design a wide variety of small protein folds while sampling shape diversity. We designed and evaluated stability of about 30,000 de novo protein designs of eight different folds. Among these designs, about 6,200 stable proteins were identified, including some predicted to have a first-of-its-kind minimalized thioredoxin fold. Obtained data revealed protein folding rules for structural features such as helix-connecting loops. Beyond serving as a resource for protein engineering, this massive and diverse dataset also provides training data for machine learning. We developed an accurate classifier to predict the stability of our designed proteins. The methods and the wide range of protein shapes provide a basis for designing new protein functions without compromising stability.

PubMed: 36418330
DOI: 10.1038/s41467-022-34937-8

実験手法

SOLUTION NMR