1qtg
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(New page: 200px<br /><applet load="1qtg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qtg" /> '''AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE M...)
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Revision as of 22:51, 20 November 2007
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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 Yersinia phage py54. 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 Wed Nov 21 00:58:16 2007
