1GTO

HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT

1GTO の概要

• エントリーDOI: 10.2210/pdb1gto/pdb
• 分子名称: ROP (2 entities in total)
• 機能のキーワード: transcription regulation, turn, helix packing, crystal contacts
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 20975.11

構造登録者

Agrawal, V.,Predki, P.,Regan, L.,Brunger, A.T. (登録日: 1996-04-23, 公開日: 1997-01-27, 最終更新日: 2024-02-07)

主引用文献

Predki, P.F.,Agrawal, V.,Brunger, A.T.,Regan, L.
Amino-acid substitutions in a surface turn modulate protein stability.
Nat.Struct.Biol., 3:54-58, 1996

PubMed Abstract: A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects.

PubMed: 8548455
DOI: 10.1038/nsb0196-54

実験手法

X-RAY DIFFRACTION (1.82 Å)