1ss1: Difference between revisions
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'''STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES''' | '''STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES''' | ||
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[[Category: Religa, T L.]] | [[Category: Religa, T L.]] | ||
[[Category: Sato, S.]] | [[Category: Sato, S.]] | ||
[[Category: | [[Category: Immunoglobulin-binding protein]] | ||
[[Category: | [[Category: Three-helical bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:04:33 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:04, 3 May 2008
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| 1ss1, 26 NMR models () | |||||||||
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| Gene: | SPA (Staphylococcus aureus) | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES
OverviewOverview
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 StructureAbout this Structure
1SS1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 09:04:33 2008