1QTG
AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR
Summary for 1QTG
Entry DOI | 10.2210/pdb1qtg/pdb |
Related | 1ARR 1PAR |
NMR Information | BMRB: 4540 |
Descriptor | Transcriptional repressor arc (1 entity in total) |
Functional Keywords | beta-sheet, right-handed helix, structural change, gene regulation |
Biological source | Lederbergvirus P22 |
Total number of polymer chains | 2 |
Total formula weight | 12476.54 |
Authors | Cordes, M.H.J.,Walsh, N.P.,McKnight, C.J.,Sauer, R.T. (deposition date: 1999-06-27, release date: 1999-07-12, Last modification date: 2024-05-22) |
Primary citation | Cordes, M.H.,Walsh, N.P.,McKnight, C.J.,Sauer, R.T. Evolution of a protein fold in vitro. Science, 284:325-327, 1999 Cited by PubMed Abstract: 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. PubMed: 10195898DOI: 10.1126/science.284.5412.325 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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