Extended Data Fig. 6: Structural analysis of diUb dimeric complex.
From: Structural basis for E4 enzyme Ufd2-catalyzed K48/K29 branched ubiquitin chains
a-b, Structure model of diUb dimeric complex with semi-transparent cryo-EM density maps and rectangular regions correspond to the interfaces shown in (e). c, Interface between core regionA and core regionB shown in (f). d, Representative two-dimensional (2D) characteristic of the diUb dimeric complex. e, Expanded view of the head-to-head assembled dimeric Ufd2. f, Expanded view of the formation of dimeric Ufd2 mediated by the dimeric helix (residue 419-439). g, Cryo-EM density of diUb dimeric complex at level 0.02, the density is represented in a translucent manner and fitted in two diUb monomeric complex (PDB:9KHS) and two N-terminal variable domain of Ufd2 (PDB: 3M62). h, A side view of the cryo-EM density of the di-ubiquitin dimeric complex. i. A close-up view of the N-terminal region of the di-ubiquitin dimeric complex reveals that the N-terminal variable domains of Ufd2 in the two protomers do not conflict.
