Fig. 2: Cryo-EM structures representing TRIP12-catalyzed polyubiquitylation.
From: TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains
a, Chemical structures of native intermediate (left) and the stable mimic (right) involved in generating K29 linkages. b, Schematic of TRIP12 domains. IDR, intrinsically disordered region; ARM, armadillo repeats with tandem Ub-binding regions; HEL-UBL, helical scaffold and Ub-like domain; HECT, catalytic domain with N- and C-lobes. c, Cryo-EM map (DeepEMhancer-sharpened) representative of TRIP12ΔN forming a K29/K48 branched ubiquitin chain. TRIP12 domains are colored according to scheme in b, ubiquitins according to scheme in a. d, Similar to c, but for complex representing the formation of a K29-linked ubiquitin chain.
