1ss1: Difference between revisions

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[[Image:1ss1.gif|left|200px]]
{{Seed}}
[[Image:1ss1.png|left|200px]]


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{{STRUCTURE_1ss1|  PDB=1ss1  |  SCENE=  }}  
{{STRUCTURE_1ss1|  PDB=1ss1  |  SCENE=  }}  


'''STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES'''
===STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_15069202}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15069202 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15069202}}


==About this Structure==
==About this Structure==
1SS1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SS1 OCA].  
1SS1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SS1 OCA].  


==Reference==
==Reference==
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[[Category: Immunoglobulin-binding protein]]
[[Category: Immunoglobulin-binding protein]]
[[Category: Three-helical bundle]]
[[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 Mon Jul 28 10:24:43 2008''

Revision as of 07:24, 28 July 2008

File:1ss1.png


Drag the structure with the mouse to rotate
1ss1, 26 NMR models (default scene)
Gene: SPA (Staphylococcus aureus)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES

Template:ABSTRACT PUBMED 15069202

About this Structure

1SS1 is a Single protein structure of sequence from Staphylococcus aureus. Full experimental 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 Mon Jul 28 10:24:43 2008

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