3Q7Y

Crystal structure of K15R/E18D/Y22W/H41G/F44W/E51D/E53P/K57R/E60D/Y64W/H82G/F85W/E90D/E94P/K98R/E101D/Y108W/H129G/F132W/E137D Symfoil-4P: de novo designed beta-trefoil architecture with symmetric primary structure

3Q7Y の概要

• エントリーDOI: 10.2210/pdb3q7y/pdb
• 関連するPDBエントリー: 1JQZ 3O4D 3Q7W 3Q7X
• 分子名称: De novo designed beta-trefoil architecture with symmetric primary structure (2 entities in total)
• 機能のキーワード: beta-trefoil, de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14580.71

構造登録者

Blaber, M.,Lee, J. (登録日: 2011-01-05, 公開日: 2012-01-11, 最終更新日: 2024-02-21)

主引用文献

Longo, L.M.,Lee, J.,Blaber, M.
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.
Proc.Natl.Acad.Sci.USA, 110:2135-2139, 2013

PubMed Abstract: A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 "prebiotic" α-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a "foldable set"--that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two "primitive" versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment.

PubMed: 23341608
DOI: 10.1073/pnas.1219530110

実験手法

X-RAY DIFFRACTION (1.45 Å)