Extended Data Fig. 8: Coiled-coil docking factors potentially contribute to axonemal asymmetry.
From: Axonemal structures reveal mechanoregulatory and disease mechanisms
a, Atomic models of the FAP189 and FAP57 homodimers. Other axonemal complexes are omitted for clarity. FAP189 forms an L-shaped coiled coil that occupies the interprotofilament cleft between protofilaments A04 and A05. b, Fit of FAP189 atomic model into the cryo-EM map. Labeled amino acids are denoted below by bold font in the multiple sequence alignment of FAP189 with its paralogs FAP58 and MBO2. The conserved sequence ALSXXLENP, highlighted in red, corresponds to residues that interact with FAP100 of the MIA complex (see Extended Data Fig. 2b). c, Agreement of cryo-EM sidechain density with the atomic model of FAP57. Residues labeled in the model are denoted by bold font in the multiple sequence alignment below. d, Domain architecture of FAP189, FAP58, and MBO2. e, Phylogenetic tree showing the relationship between FAP189, FAP58, and MBO2. FAP189 and FAP58 share 80% sequence identity. f, Domain architecture of FAP57, FBB7 and FAP331, which are composed of tandem N-terminal β-propellers and a long, helical C-terminal region. g, Phylogenetic tree showing the relationship between FAP57, FBB7, and FAP331.
