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. 2017 Aug 7;3(8):830–838. doi: 10.1021/acscentsci.7b00252

Figure 1.

Figure 1

The proteasome. (A) α- and β-subunits are arranged in rings of seven. The catalytically active subunits are β1 (CL), β2 (TL), and β5 (ChTL). (B) The 20S CP comprises 28 subunits grouped into four rings stacked in an αββα pattern and forming the catalytic chamber. The three different 20S CPs are the cCP, iCP, and tCP and vary by their catalytic subunits. (C) Schematic assembly of the two proteasome lids, the 11S cap and the 19S RP. The 11S cap is formed out of seven subunits and acts in a ubiquitin- and ATP-independent manner. The 19S RP can be divided into the base (10 subunits) and the lid (9 subunits) which inherits the deubiquinating enzyme Rpn11. (D) Different proteasome assemblies have been identified, thus far. The 26S proteasome comprises the 20S CP capped with two 19S RP. The 11S cap can either associate with the free end of a 19S–20S complex to form a hybrid proteasome or bind to both sides of the 20S CP.