1Z7Q

Crystal structure of the 20s proteasome from yeast in complex with the proteasome activator PA26 from Trypanosome brucei at 3.2 angstroms resolution

Summary for 1Z7Q

• Entry DOI: 10.2210/pdb1z7q/pdb
• Related: 1FNT
• Descriptor: Proteasome component C7-alpha, Proteasome component PUP3, Proteasome component C11, ... (15 entities in total)
• Functional Keywords: 20s, proteasome, pa26, activator, multi-catalytic protease, hydrolase-hydrolase activator complex, hydrolase/hydrolase activator
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm : P21243 P25451 P22141 P30656 P23724 P30657 P23639 P23638 P40303 P32379 P40302 P21242 P38624 P25043
• Total number of polymer chains: 42
• Total formula weight: 1079543.87

Authors

Forster, A.,Whitby, F.G.,Hill, C.P. (deposition date: 2005-03-26, release date: 2005-08-09, 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 (3.22 Å)