Extended Data Fig. 7: Impact of palmitoyl-CoA addition on ACC–citrate filaments and architecture of ACC–BRCT.
From: Structural basis for regulation of human acetyl-CoA carboxylase
a, Negative stain electron microscopy micrographs of ACC–citrate filaments treated with increasing concentrations of palmitoyl-CoA. At a 1:1 molar ratio of ACC–citrate monomer to palmitoyl-CoA, filaments show no differences to ACC–citrate filaments. At 1:10 molar ratio, ACC–citratepalm filaments are observed. At 1:100 molar ratio, filaments dissolve. b, Top, domain organization of human ACC. Bottom left, enlarged negative stain electron micrograph of ACC–citrate filament with surface representation of the model coloured according to domains. Bottom right, electron micrograph of a ACC–citratepalm filament and interpretation by a plausible model derived from ACC–citrate filaments by disrupting the BC domain dimers and flipping out of the BC domain. c, Surface representation of ACC–BRCT with components of a single node coloured as in Fig. 3a. Domains of three molecules (A, B and B−1) add parts to the node. d, Same view as in c, but the domains are coloured according to the domain colour scheme in b. e, Same view as in c, with the CDC2 domains coloured according to domain colour scheme. These domains constitute the connecting arms between adjacent nodes. f, Surface representation of two consecutive dimers within one helix strand. Left, view without BRCT domains; the phosphosite loops are labelled. Right, view with dimeric BRCT domains establishing the connections between two dimers. g, Enlarged view of the phosphosite loop-BRCT interaction area, illustrating minimal contacts between the two CDC1 domains and between the filament strands and the BRCT domains. The interaction is governed by binding of the phosphosite loop to the dimeric BRCT.
