2F49
Crystal structure of Fus3 in complex with a Ste5 peptide
Summary for 2F49
| Entry DOI | 10.2210/pdb2f49/pdb |
| Related | 2B9F 2B9H 2B9I 2B9J |
| Descriptor | Mitogen-activated protein kinase FUS3, STE5 peptide, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | protein-petide complex, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Nucleus: P16892 |
| Total number of polymer chains | 3 |
| Total formula weight | 85423.05 |
| Authors | Remenyi, A. (deposition date: 2005-11-22, release date: 2006-03-28, Last modification date: 2023-08-23) |
| Primary citation | Bhattacharyya, R.P.,Remenyi, A.,Good, M.C.,Bashor, C.J.,Falick, A.M.,Lim, W.A. The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway Science, 311:822-826, 2006 Cited by PubMed Abstract: Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties. PubMed: 16424299DOI: 10.1126/science.1120941 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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