Literature summary for 5.6.1.5 extracted from

Tomko, R.J.; Funakoshi, M.; Schneider, K.; Wang, J.; Hochstrasser, M.
Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly (2010), Mol. Cell, 38, 393-403.

Crystallization (Commentary)

Crystallization (Comment)	Organism
eukaryotic ATPases form a heterohexameric ring with the arrangement Rpt1-Rpt2-Rpt6-Rpt3-Rpt4-Rpt5 (Rp, regulatory particles) in fully assembled proteasomes. This quaternary organization clarifies the functional overlap of specific RP assembly chaperones and leads to the identification of a potential RP assembly intermediate that includes four ATPases (Rpt6-Rpt3-Rpt4-Rpt5) and their cognate chaperones Rpn14, Nas6, and Nas2	Saccharomyces cerevisiae S288c

Crystallization (Comment)

Organism

eukaryotic ATPases form a heterohexameric ring with the arrangement Rpt1-Rpt2-Rpt6-Rpt3-Rpt4-Rpt5 (Rp, regulatory particles) in fully assembled proteasomes. This quaternary organization clarifies the functional overlap of specific RP assembly chaperones and leads to the identification of a potential RP assembly intermediate that includes four ATPases (Rpt6-Rpt3-Rpt4-Rpt5) and their cognate chaperones Rpn14, Nas6, and Nas2

Saccharomyces cerevisiae S288c

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae S288c	-	-	-

Subunits

Subunits	Comment	Organism
hexamer	four of the six ATPase subunits and three of the four regulatory particles (RP) base assembly chaperones form a potential assembly intermediate	Saccharomyces cerevisiae S288c

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Release 2023.1 (January 2023)