2WQG

SAP domain from Tho1: L31W (fluorophore) mutant

Summary for 2WQG

• Entry DOI: 10.2210/pdb2wqg/pdb
• Related: 1H1J
• Descriptor: PROTEIN THO1 (1 entity in total)
• Functional Keywords: unknown function
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 5655.26

Authors

Dodson, C.A.,Ferguson, N.,Rutherford, T.J.,Johnson, C.M.,Fersht, A.R. (deposition date: 2009-08-21, release date: 2010-02-16, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR