Fig. 4: CsoS2 C-terminal fragments interacts with shell proteins.
From: Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly
a Schematic of four CsoS2 constructs. b Quantification of shell assembly from different CsoS2 constructs. The ratios of assembled shell and free shell proteins are quantified from western blot experiments (n = 3, see also Fig. S9). The ratios are presented as mean values +/− SEM. 4A-1A denotes the CsoS4A-CsoS1A mini-shell. c Gallery of different shells formed in these constructs with hexamer in blue and pentamer in magenta. d Distribution of different shells in the four CsoS2 constructs as calculated from cryo-EM analysis; the number of particles for each shell is indicated in the Supplementary Tables 1 and 2. Source data are provided as a Source data file. e A schematic model of CsoS2 interacting with shell proteins and Rubisco using the C-terminal domain and N-terminal domain, respectively. Enlarged view shows the interactions of each fragment in CsoS2 C-terminal domain, F1, F2 and F3, with shell capsomers in the assembly.
