2FA2

Crystal structure of Fus3 without a peptide from Ste5

Summary for 2FA2

• Entry DOI: 10.2210/pdb2fa2/pdb
• Related: 2F49 2F9G
• Descriptor: Mitogen-activated protein kinase FUS3, THIOCYANATE ION (3 entities in total)
• Functional Keywords: map kinase, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P16892
• Total number of polymer chains: 2
• Total formula weight: 81966.59

Authors

Bhattacharyya, R.P.,Remenyi, A.,Good, M.C.,Bashor, C.J.,Falick, A.M.,Lim, W.A. (deposition date: 2005-12-06, release date: 2006-03-28, Last modification date: 2023-08-30)

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

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: 16424299
DOI: 10.1126/science.1120941

Experimental method

X-RAY DIFFRACTION (2.85 Å)