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The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions.

Förster A, Masters EI, Whitby FG, Robinson H, Hill CP
Mol Cell 18 589-99 (2005)
Related entries: 1yar, 1yau, 1z7q

Cited: 148 times
EuropePMC logo PMID: 15916965

Abstract

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.

Reviews - 1ya7 mentioned but not cited (1)

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Articles - 1ya7 mentioned but not cited (12)

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