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1rkn

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{{STRUCTURE_1rkn| PDB=1rkn | SCENE= }}
{{STRUCTURE_1rkn| PDB=1rkn | SCENE= }}
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'''Solution structure of 1-110 fragment of Staphylococcal Nuclease with G88W mutation'''
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===Solution structure of 1-110 fragment of Staphylococcal Nuclease with G88W mutation===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17172296}}
==About this Structure==
==About this Structure==
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1RKN 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=1RKN OCA].
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1RKN 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=1RKN OCA].
==Reference==
==Reference==
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[[Category: G88w110]]
[[Category: G88w110]]
[[Category: Staphylococcal nuclease]]
[[Category: Staphylococcal nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:36:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:59:02 2008''

Revision as of 11:59, 29 July 2008

Image:1rkn.png

Template:STRUCTURE 1rkn

Solution structure of 1-110 fragment of Staphylococcal Nuclease with G88W mutation

Template:ABSTRACT PUBMED 17172296

About this Structure

1RKN is a Single protein structure of sequence from Staphylococcus aureus. Full experimental information is available from OCA.

Reference

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 Tue Jul 29 14:59:02 2008

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