2OVN
NMR structure of the GCN4 trigger peptide
Summary for 2OVN
| Entry DOI | 10.2210/pdb2ovn/pdb |
| Descriptor | General control protein GCN4 (1 entity in total) |
| Functional Keywords | gcn4, coiled-coil, trigger peptide, transcription |
| Cellular location | Nucleus: P03069 |
| Total number of polymer chains | 1 |
| Total formula weight | 2016.30 |
| Authors | Matousek, W.M.,Alexandrescu, A.T. (deposition date: 2007-02-14, release date: 2007-04-03, Last modification date: 2024-05-22) |
| Primary citation | Steinmetz, M.O.,Jelesarov, I.,Matousek, W.M.,Honnappa, S.,Jahnke, W.,Missimer, J.H.,Frank, S.,Alexandrescu, A.T.,Kammerer, R.A. Molecular basis of coiled-coil formation. Proc.Natl.Acad.Sci.Usa, 104:7062-7067, 2007 Cited by PubMed Abstract: Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed "trigger sequence," that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation. PubMed: 17438295DOI: 10.1073/pnas.0700321104 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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