Extended Data Fig. 5: Conservation analysis for structure comparison.
a) ConSurf analysis for all COPI and AP-2 subunits present in A. th. A floating average of 5 residues was calculated from the per-residue ConSurf score. This average was then colored green, if the value was below 5 and the sequence therefore variable, or it was colored purple if the score was above 5 and therefore conserved. b) The AP-2β appendages are the least conserved domains in the analysis performed in a). To demonstrate the structural conservation for the AP-2β appendages, structural models of the Arabidopsis AP-2β subunits were taken from the AlphaFold2 database and the appendage domains were aligned to the published human cryo EM model (PDB 6YAI) with UCSF ChimeraX. The AP-2β appendages of both Arabidopsis alleles are structurally nearly identical to their human counterpart, as is evident from their RMSD values. c) To demonstrate the conservation of the disordered TML linker, we performed a ConSurf analysis for TML as in a). This conserved 210 residue linker was replaced with the shorter 38 residue long AP-2μ linker from Arabidopsis in the TML-AP-2μ chimera. The legend below c) applies to a) and c). The scale bar represents 250 residues.
