4QKR

Crystal Structure of 6xTyr/PV2: de novo designed beta-trefoil architecture with symmetric primary structure (L22Y/L44Y/L64Y/L85Y/L108Y/L132Y, Primitive Version 2)

4QKR の概要

• エントリーDOI: 10.2210/pdb4qkr/pdb
• 関連するPDBエントリー: 4D8H 4QKS
• 分子名称: DE NOVO PROTEIN 6XTYR/PV2, IMIDAZOLE (3 entities in total)
• 機能のキーワード: simplified protein design, prebiotic protein, beta-trefoil, de novo protein
• 由来する生物種: Synthetic
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14691.73

構造登録者

Longo, L.M.,Blaber, M.,Tenorio, C.A. (登録日: 2014-06-09, 公開日: 2015-01-14, 最終更新日: 2024-02-28)

主引用文献

Longo, L.M.,Tenorio, C.A.,Kumru, O.S.,Middaugh, C.R.,Blaber, M.
A single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.
Protein Sci., 24:27-37, 2015

PubMed Abstract: The halophile environment has a number of compelling aspects with regard to the origin of structured polypeptides (i.e., proteogenesis) and, instead of a curious niche that living systems adapted into, the halophile environment is emerging as a candidate "cradle" for proteogenesis. In this viewpoint, a subsequent halophile-to-mesophile transition was a key step in early evolution. Several lines of evidence indicate that aromatic amino acids were a late addition to the codon table and not part of the original "prebiotic" set comprising the earliest polypeptides. We test the hypothesis that the availability of aromatic amino acids could facilitate a halophile-to-mesophile transition by hydrophobic core-packing enhancement. The effects of aromatic amino acid substitutions were evaluated in the core of a "primitive" designed protein enriched for the 10 prebiotic amino acids (A,D,E,G,I,L,P,S,T,V)-having an exclusively prebiotic core and requiring halophilic conditions for folding. The results indicate that a single aromatic amino acid substitution is capable of eliminating the requirement of halophile conditions for folding of a "primitive" polypeptide. Thus, the availability of aromatic amino acids could have facilitated a critical halophile-to-mesophile protein folding adaptation-identifying a selective advantage for the incorporation of aromatic amino acids into the codon table.

PubMed: 25297559
DOI: 10.1002/pro.2580

実験手法

X-RAY DIFFRACTION (1.746 Å)