1ya7
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Implications for interactions of proteasome with PAN and PA700 from the 1.9 A structure of a proteasome-11S activator complex
OverviewOverview
Proteasomes are cylindrical structures that function in multiple cellular processes by degrading a wide variety of cytosolic and nuclear proteins. Substrate access and product release from the enclosed catalytic chamber occurs through axial pores that are opened by activator complexes. Here, we report high-resolution structures of wild-type and mutant archaeal proteasomes bound to the activator PA26. These structures support the proposal that an ordered open conformation is required for proteolysis and that its formation can be triggered by outward displacement of surrounding residues. The structures and associated biochemical assays reveal the mechanism of binding, which involves an interaction between the PA26 C terminus and a conserved lysine. Surprisingly, biochemical observations implicate an equivalent interaction for the unrelated ATP-dependent activators PAN and PA700.
About this StructureAbout this Structure
1YA7 is a Protein complex structure of sequences from Thermoplasma acidophilum and Trypanosoma brucei with and as ligands. Active as Proteasome endopeptidase complex, with EC number 3.4.25.1 Full crystallographic information is available from OCA.
ReferenceReference
The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions., Forster A, Masters EI, Whitby FG, Robinson H, Hill CP, Mol Cell. 2005 May 27;18(5):589-99. PMID:15916965
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