1qtg
From Proteopedia
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[[Image:1qtg.gif|left|200px]] | [[Image:1qtg.gif|left|200px]] | ||
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'''AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR''' | '''AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR''' | ||
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[[Category: Sauer, R T.]] | [[Category: Sauer, R T.]] | ||
[[Category: Walsh, N P.]] | [[Category: Walsh, N P.]] | ||
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- | [[Category: | + | [[Category: Right-handed helix]] |
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:07 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 03:41, 3 May 2008
AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR
Overview
A "switch" mutant of the Arc repressor homodimer was constructed by interchanging the sequence positions of a hydrophobic core residue, leucine 12, and an adjacent surface polar residue, asparagine 11, in each strand of an intersubunit beta sheet. The mutant protein adopts a fold in which each beta strand is replaced by a right-handed helix and side chains in this region undergo significant repacking. The observed structural changes allow the protein to maintain solvent exposure of polar side chains and optimal burial of hydrophobic side chains. These results suggest that new protein folds can evolve from existing folds without drastic or large-scale mutagenesis.
About this Structure
1QTG is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.
Reference
Evolution of a protein fold in vitro., Cordes MH, Walsh NP, McKnight CJ, Sauer RT, Science. 1999 Apr 9;284(5412):325-8. PMID:10195898 Page seeded by OCA on Sat May 3 06:41:07 2008