Extended Data Figure 4 : Structural comparisons of domains in LCC with related enzymes.

From: Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase

Extended Data Figure 4

a, Stereo drawing of the overlay of the structure of the BC domain dimer of MapLCC (in colour) with that of BC subunit dimer of E. coli ACC (in grey)20. The bound positions of biotin (black) and ADP (green) in the E. coli BC structure are also shown. The two-fold axis of the dimer is indicated by the black oval. With the two monomers at the bottom overlaid, a difference of 21° in the orientations of the two monomers at the top is observed. Most of the B domain of BC is ordered in one of the two monomers of MapLCC. In the other monomer, only weak electron density is observed for a few segments, and the B domain is not modelled. b, Overlay of the structures of the CT domain hexamer of MapLCC (in colour) and the β subunit of PCC (in grey)10. Each enzyme is highly conserved across species; the overlay should therefore be meaningful. c, Stereo drawing of the overlay of the CT domain dimer of MapLCC (in colour) and the β subunit of PCC (in grey). The view is down the red arrow in b. The bound position of biotin in the holoenzyme is shown in black. The position of CoA is modelled on that of CoA bound in the active site of the CT domain of yeast ACC29. d, Plot of the temperature factor value of each Cα atom in the two monomers (in red and blue). Several linker regions with high temperature factor values are indicated.