Extended Data Fig. 5: Comparison of the Preholoproteasome and 20S Structures.
From: Structure of the preholoproteasome reveals late steps in proteasome core particle biogenesis
a, Molecular model of the 20S CP. b-c, Primary cryo-EM densities of the 20S CP (panel B) and preholoproteasome (panel C). The boxed region in the 20S CP shows excellent resolution at the β4/β5 interface, in contrast to the preholoproteasome where there is marked loss of resolution which likely reflects subunit flexibility. d, The β5 catalytic triad appears largely intact in the 20S CP, suggesting that other, potentially dynamic aspects, of catalytic function are impaired in the pre1-1, 4-1 mutant. The cryo-EM density in panel D is displayed with a map contour of 0.67 and a Zone radius of 3.0 Å.
