Extended Data Fig. 8: Analysis of the architecture of ACC–BRCT filaments.
From: Structural basis for regulation of human acetyl-CoA carboxylase
a, Surface representation of dimers of ACC–BRCT, C. thermophilum (Ct) ACC CD–CT, and ACC–citrate, in the same relative orientation and coloured according to the sequence scheme shown below. b, CT-based overlay of the three structures, illustrating the rotations (indicated by arrows) of the CDC2 domains of ACC–citrate and CtACC relative to CDC2 of ACC–BRCT. CD–CT of ACC–BRCT, ACC–citrate and CtACC are shown in full colour, light grey and dark grey, respectively. Helix C2α1 is labelled. c, CDC2-based overlay of the three structures, representing the displacement (indicated) of CDC1 of ACC–citrate and CtACC relative to CDC1 of ACC–BRCT. Colouring as in b. CDL was omitted for clarity, and helix C1α1 is labelled. d, CDL-based overlay of the three structures, illustrating the displacement of the CDN of ACC–citrate and CtACC relative to CDN of ACC–BRCT. Colouring as in b. The four-helix bundle of helices Nα3–Nα6 is labelled. The range of displacements of the ends of the bundle is indicated by arrows. e, BC, BT and CDN domains of ACC–BRCT filament together with the electron microscopy map at a low contour level to visualize less well-ordered regions and to illustrate the placement of the B-domain cap of the BC domain in the clamp-like CDN domain. f, Overlay of CDN, BT and BCCP domains from ACC–BRCT and ACC–citrate, revealing a conserved conformation. g, CDN, BT and BCCP domains in the ACC–BRCT filament are shown together with the electron microscopy map at low contour level to visualize the poorly ordered BCCP domain. Maps in e and g are shown at contour level of 0.007. h, The SEC–MALS elution profiles show the molecular mass (right axis) and the scattering intensity (Rayleigh ratio) at the 90° detector (left axis) of BRCT domains bound to the indicated ACC peptides. Elution for BRCT and the BRCT–ACC_p1 complex correspond to a mostly monomeric species with a dimeric subpopulation in fast equilibrium with an average molecular mass of 31.8 kDa and 34.8 kDa, respectively. The elution of BRCT–ACC_p2 with a molecular mass of 51.1 kDa indicates a strong increase in the population of dimeric BRCT-peptide species.
