2wqg | pdb_00002wqg

SAP domain from Tho1: L31W (fluorophore) mutant

spinqualitylabelsall models 2wqg, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wqg is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1h1j Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Engineering a two-helix bundle protein for folding studies.,Dodson CA, Ferguson N, Rutherford TJ, Johnson CM, Fersht AR Protein Eng Des Sel. 2010 May;23(5):357-64. Epub 2010 Feb 3. PMID:20130106 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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