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. Author manuscript; available in PMC: 2014 Jan 23.
Published in final edited form as: J Mol Biol. 2012 Nov 9;425(2):199–213. doi: 10.1016/j.jmb.2012.11.001

Figure 2. The 26S proteasome can be separated into three stably associated subcomplexes.

Figure 2

A) Cryo-EM reconstruction of the eukaryotic proteasome holoenzyme with the core particle in grey and the regulatory particle multicolored 33. B) Individual sub-complexes of the 26S proteasome. The regulatory particle can be separated into two stable sub-complexes, the lid and the base. The base consists of the AAA+ ATPase subunits Rpt1-6, (cyan), two large torroidal subunits, Rpn1 (purple) and Rpn2 (light blue), and the ubiquitin receptor Rpn13 (orange). The lid contains six PCI-domain subunits (multicolored) along with the essential DUB Rpn11 (green) and the ubiquitin receptor Rpn10 (yellow). A central cross-section of the core particle (grey) is shown to allow visualization of the barrel-shaped central cavity.