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'''Solution structure of 1-110 fragment of staphylococcal nuclease with V66W mutation''' | '''Solution structure of 1-110 fragment of staphylococcal nuclease with V66W mutation''' | ||
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[[Category: Xie, T.]] | [[Category: Xie, T.]] | ||
[[Category: Ye, K.]] | [[Category: Ye, K.]] | ||
[[Category: | [[Category: Ob-fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:25:56 2008'' | |||
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Revision as of 03:25, 4 May 2008
Solution structure of 1-110 fragment of staphylococcal nuclease with V66W mutation
OverviewOverview
Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease (SNase110) have been studied by various biophysical and NMR methods. Samples of G-88W- and V-66W-mutant SNase110, namely G-88W110 and V-66W110, in aqueous solution and SNase110 in 2.0 M TMAO are adopted in this study. The unfolding transitions and folded conformations of the three SNase fragments were detected by far- and near-ultraviolet circular dichroism and intrinsic tryptophan fluorescence measurements. The tertiary structures and internal motions of the fragments were determined by NMR spectroscopy. Both G-88W and V-66W single mutations as well as a small organic osmolyte (Trimethylamine N-oxide, TMAO) can fold the fragment into a native-like conformation. However, the tertiary structures of the three fragments exhibit different degrees of folding stability and compactness. G-88W110 adopts a relatively rigid structure representing a most stable native-like beta-subdomain conformation of the three fragments. V-66W110- and TMAO-stabilized SNase110 produce less compact structures having a less stable "beta-barrel" structural region. The different folding status accounts for the different backbone dynamic and urea-unfolding transition features of the three fragments. The G-20I/G-29I-mutant variants of the three fragments have provided the evidence that the folding status is correlated closely to the packing of the beta-strands in the beta-barrel of the fragments. The native-like beta-barrel structural region acts as a nonlocal nucleus for folding the fragment. The tertiary folding of the three fragments is initiated by formation of the local nucleation sites at two beta-turn regions, I-18-D-21 and Y-27-Q-30, and developed by the formation of a nonlocal nucleation site at the beta-barrel region. The formation of beta-barrel and overall structure is concerted, but the level of cooperativity is different for the three 1-110 residues SNase fragments.
About this StructureAbout this Structure
2F3V is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease., Xie T, Liu D, Feng Y, Shan L, Wang J, Biophys J. 2007 Mar 15;92(6):2090-107. Epub 2006 Dec 15. PMID:17172296 Page seeded by OCA on Sun May 4 03:25:56 2008