1YA7

Implications for interactions of proteasome with PAN and PA700 from the 1.9 A structure of a proteasome-11S activator complex

Summary for 1YA7

• Entry DOI: 10.2210/pdb1ya7/pdb
• Descriptor: Proteasome alpha subunit, Proteasome beta subunit, proteasome activator protein PA26, ... (6 entities in total)
• Functional Keywords: archaeal proteasome, pa26, copmlex, open gate, hydrolase-hydrolase activator complex, hydrolase/hydrolase activator
• Biological source: Thermoplasma acidophilum; More
• Cellular location: Cytoplasm (By similarity): P25156 P28061
• Total number of polymer chains: 21
• Total formula weight: 534072.45

Authors

Forster, A.,Masters, E.I.,Whitby, F.G.,Robinson, H.,Hill, C.P. (deposition date: 2004-12-17, release date: 2005-07-26, Last modification date: 2023-08-23)

Primary citation

Forster, A.,Masters, E.I.,Whitby, F.G.,Robinson, H.,Hill, C.P.
The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions.
Mol.Cell, 18:589-599, 2005

PubMed 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.

PubMed: 15916965
DOI: 10.1016/j.molcel.2005.04.016

Experimental method

X-RAY DIFFRACTION (2.3 Å)