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

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

Content Provider	Semantic Scholar
Author	Foerster, Andreas Masters, Eugene I. Whitby, Frank G. Robinson, Howard Hill, Christopher P.
Copyright Year	2005
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.
File Format	PDF HTM / HTML
DOI	10.1016/j.molcel.2005.04.016
PubMed reference number	15916965
Journal	Medline
Volume Number	18
Issue Number	5
Alternate Webpage(s)	http://www.biochem.utah.edu/hill/publications/63s.pdf
Alternate Webpage(s)	http://www.biochem.utah.edu/hill/publications/63.pdf
Alternate Webpage(s)	https://static1.squarespace.com/static/5dd5a1ab47b52c5c5980efb4/t/5e1d03566b4ecf142ad67ace/1578959703644/63.pdf
Alternate Webpage(s)	http://biochem.web.utah.edu/hill/publications/63.pdf
Alternate Webpage(s)	http://biochem.web.utah.edu/hill/publications/63s.pdf
Alternate Webpage(s)	https://doi.org/10.1016/j.molcel.2005.04.016
Journal	Molecular cell
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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