Fig. 5 | Nature Communications

Fig. 5

From: Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome

Fig. 5

Cryo-EM densities of the nucleotides in the SD1 and SD2 states of the ATP-γ-S-bound RP–CP subcomplex. a, c Overview of the nucleotide-binding sites in the AAA-ATPase heterohexamer of the ATP-γ-S-bound human 26S proteasome in the SD1 (a) and SD2 (c) states. Bound nucleotides are shown in a stick representation superimposed over their respective cryo-EM densities in a blue mesh representation. b, d Close-up views of nucleotide conformations in the nucleotide-binding sites in the SD1 (b) and SD2 (d) states. ATP-γ-S was modeled into the nucleotide densities of four Rpt subunits in each state

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