Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae S288c | - |
- |
- |
Subunits | Comment | Organism |
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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 |