3PG0

Crystal structure of designed 3-fold symmetric protein, ThreeFoil

3PG0 の概要

• エントリーDOI: 10.2210/pdb3pg0/pdb
• 分子名称: ThreeFoil, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: symmetric design, beta-trefoil, engineered module, sugar binding, de novo protein
• 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: 18896.30

構造登録者

Lobsanov, Y.D.,Broom, A.,Howell, P.L.,Rose, D.R.,Meiering, E.M. (登録日: 2010-10-29, 公開日: 2011-12-21, 最終更新日: 2023-09-06)

主引用文献

Broom, A.,Doxey, A.C.,Lobsanov, Y.D.,Berthin, L.G.,Rose, D.R.,Howell, P.L.,McConkey, B.J.,Meiering, E.M.
Modular evolution and the origins of symmetry: reconstruction of a three-fold symmetric globular protein.
Structure, 20:161-171, 2012

PubMed Abstract: The high frequency of internal structural symmetry in common protein folds is presumed to reflect their evolutionary origins from the repetition and fusion of ancient peptide modules, but little is known about the primary sequence and physical determinants of this process. Unexpectedly, a sequence and structural analysis of symmetric subdomain modules within an abundant and ancient globular fold, the β-trefoil, reveals that modular evolution is not simply a relic of the ancient past, but is an ongoing and recurring mechanism for regenerating symmetry, having occurred independently in numerous existing β-trefoil proteins. We performed a computational reconstruction of a β-trefoil subdomain module and repeated it to form a newly three-fold symmetric globular protein, ThreeFoil. In addition to its near perfect structural identity between symmetric modules, ThreeFoil is highly soluble, performs multivalent carbohydrate binding, and has remarkably high thermal stability. These findings have far-reaching implications for understanding the evolution and design of proteins via subdomain modules.

PubMed: 22178248
DOI: 10.1016/j.str.2011.10.021

実験手法

X-RAY DIFFRACTION (1.62 Å)