2F4K

Chicken villin subdomain HP-35, K65(NLE), N68H, K70(NLE), PH9

2F4K の概要

• エントリーDOI: 10.2210/pdb2f4k/pdb
• 関連するPDBエントリー: 1WY3 1WY4 1YRF 1YRI
• 分子名称: Villin-1 (2 entities in total)
• 機能のキーワード: villin head group subdomain, structural protein
• 細胞内の位置: Cytoplasm, cytoskeleton : P02640
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4056.71

構造登録者

Chiu, T.K.,Davies, D.R.,Kubelka, J.,Hofrichter, J.,Eaton, W.A. (登録日: 2005-11-23, 公開日: 2006-04-11, 最終更新日: 2023-11-15)

主引用文献

Kubelka, J.,Chiu, T.K.,Davies, D.R.,Eaton, W.A.,Hofrichter, J.
Sub-microsecond Protein Folding.
J.Mol.Biol., 359:546-553, 2006

PubMed Abstract: We have investigated the structure, equilibria, and folding kinetics of an engineered 35-residue subdomain of the chicken villin headpiece, an ultrafast-folding protein. Substitution of two buried lysine residues by norleucine residues stabilizes the protein by 1 kcal/mol and increases the folding rate sixfold, as measured by nanosecond laser T-jump. The folding rate at 300 K is (0.7 micros)(-1) with little or no temperature dependence, making this protein the first sub-microsecond folder, with a rate only twofold slower than the theoretically predicted speed limit. Using the 70 ns process to obtain the effective diffusion coefficient, the free energy barrier height is estimated from Kramers theory to be less than approximately 1 kcal/mol. X-ray crystallographic determination at 1A resolution shows no significant change in structure compared to the single-norleucine-substituted molecule and suggests that the increased stability is electrostatic in origin. The ultrafast folding rate, very accurate X-ray structure, and small size make this engineered villin subdomain an ideal system for simulation by atomistic molecular dynamics with explicit solvent.

PubMed: 16643946
DOI: 10.1016/j.jmb.2006.03.034

実験手法

X-RAY DIFFRACTION (1.05 Å)