1ss1
From Proteopedia
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STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES
Overview
We have assessed the published predictions of the pathway of folding of, the B domain of protein A, the pathway most studied by computer, simulation. We analyzed the transition state for folding of the, three-helix bundle protein, by using experimental Phi values on some 70, suitable mutants. Surprisingly, the third helix, which has the most stable, alpha-helical structure as a peptide fragment, is poorly formed in the, transition state, especially at its C terminus. The protein folds around a, nearly fully formed central helix, which is stabilized by extensive, hydrophobic side chain interactions. The turn connecting the poorly, structured first helix to the central helix is unstructured, but the turn, connecting the central helix to the third is in the process of being, formed as the N-terminal region of the third helix begins to coalesce. The, transition state is inconsistent with a classical framework mechanism and, is closer to nucleation-condensation. None of the published atomistic, simulations are fully consistent with the experimental picture although, many capture important features. There is a continuing need for combining, simulation with experiment to describe folding pathways, and of continued, testing to improve predictive methods.
About this Structure
1SS1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Testing protein-folding simulations by experiment: B domain of protein A., Sato S, Religa TL, Daggett V, Fersht AR, Proc Natl Acad Sci U S A. 2004 May 4;101(18):6952-6. Epub 2004 Apr 6. PMID:15069202
Page seeded by OCA on Wed Nov 21 02:37:06 2007
