1YRF

Chicken villin subdomain HP-35, N68H, pH6.7

1YRF の概要

• エントリーDOI: 10.2210/pdb1yrf/pdb
• 関連するPDBエントリー: 1wy3 1wy4 1yri
• 分子名称: Villin, SULFATE ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: villin headpiece 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: 4243.86

構造登録者

Chiu, T.K.,Kubelka, J.,Herbst-Irmer, R.,Eaton, W.A.,Hofrichter, J.,Davies, D.R. (登録日: 2005-02-03, 公開日: 2005-05-03, 最終更新日: 2024-02-14)

主引用文献

Chiu, T.K.,Kubelka, J.,Herbst-Irmer, R.,Eaton, W.A.,Hofrichter, J.,Davies, D.R.
High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.
Proc.Natl.Acad.Sci.Usa, 102:7517-7522, 2005

PubMed Abstract: The 35-residue subdomain of the villin headpiece (HP35) is a small ultrafast folding protein that is being intensely studied by experiments, theory, and simulations. We have solved the x-ray structures of HP35 and its fastest folding mutant [K24 norleucine (nL)] to atomic resolution and compared their experimentally measured folding kinetics by using laser temperature jump. The structures, which are in different space groups, are almost identical to each other but differ significantly from previously solved NMR structures. Hence, the differences between the x-ray and NMR structures are probably not caused by lattice contacts or crystal/solution differences, but reflect the higher accuracy of the x-ray structures. The x-ray structures reveal important details of packing of the hydrophobic core and some additional features, such as cross-helical H bonds. Comparison of the x-ray structures indicates that the nL substitution produces only local perturbations. Consequently, the finding that the small stabilization by the mutation is completely reflected in an increased folding rate suggests that this region of the protein is as structured in the transition state as in the folded structure. It is therefore a target for engineering to increase the folding rate of the subdomain from approximately 0.5 micros(-1) for the nL mutant to the estimated theoretical speed limit of approximately 3 micros(-1).

PubMed: 15894611
DOI: 10.1073/pnas.0502495102

実験手法

X-RAY DIFFRACTION (1.07 Å)