2WQG

SAP domain from Tho1: L31W (fluorophore) mutant

2WQG の概要

• エントリーDOI: 10.2210/pdb2wqg/pdb
• 関連するPDBエントリー: 1H1J
• 分子名称: PROTEIN THO1 (1 entity in total)
• 機能のキーワード: unknown function
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5655.26

構造登録者

Dodson, C.A.,Ferguson, N.,Rutherford, T.J.,Johnson, C.M.,Fersht, A.R. (登録日: 2009-08-21, 公開日: 2010-02-16, 最終更新日: 2024-05-15)

主引用文献

Dodson, C.A.,Ferguson, N.,Rutherford, T.J.,Johnson, C.M.,Fersht, A.R.
Engineering a Two-Helix Bundle Protein for Folding Studies.
Protein Eng.Des.Sel., 23:357-, 2010

PubMed Abstract: The SAP domain from the Saccharomyces cerevisiae THO1 protein contains a hydrophobic core and just two alpha-helices. It could provide a system for studying protein folding that bridges the gap between studies on isolated helices and those on larger protein domains. We have engineered the SAP domain for protein folding studies by inserting a tryptophan residue into the hydrophobic core (L31W) and solved its structure. The helical regions had a backbone root mean-squared deviation of 0.9 A from those of wild type. The mutation L31W destabilised wild type by 0.8 +/- 0.1 kcal mol(-1). The mutant folded in a reversible, apparent two-state manner with a microscopic folding rate constant of around 3700 s(-1) and is suitable for extended studies of folding.

PubMed: 20130106
DOI: 10.1093/PROTEIN/GZP080

実験手法

SOLUTION NMR