2f9g
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Crystal structure of Fus3 phosphorylated on Tyr182
OverviewOverview
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.
About this StructureAbout this Structure
2F9G is a Single protein structure of sequence from Saccharomyces cerevisiae with MG and ADP as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
ReferenceReference
The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway., Bhattacharyya RP, Remenyi A, Good MC, Bashor CJ, Falick AM, Lim WA, Science. 2006 Feb 10;311(5762):822-6. Epub 2006 Jan 19. PMID:16424299
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