Extended Data Fig. 2: The C. reinhardtii MIA complex contributes to the docking of inner dynein arm f (IDAf) to the doublet microtubule (DMT). | Nature

Extended Data Fig. 2: The C. reinhardtii MIA complex contributes to the docking of inner dynein arm f (IDAf) to the doublet microtubule (DMT).

From: Axonemal structures reveal mechanoregulatory and disease mechanisms

Extended Data Fig. 2: The C. reinhardtii MIA complex contributes to the docking of inner dynein arm f (IDAf) to the doublet microtubule (DMT).

a, MIA (a heterodimer of FAP73/FAP100) interacts with protofilament A05 of the DMT through a C-terminal helix of FAP100 beneath the fβ heavy chain tail. Unmodeled density of FAP100 is also shown. b, The N-terminus of the MIA coiled coil interacts with a FAP189 family member near the site of its 90° bend on the DMT surface. c, Comparison of the binding of docking complex subunits DC1/2 to ODA and MIA to IDAf. Both coiled coils bisect the helical bundles of the dynein heavy chains within the dynein cores. d, Cryo-EM map showing the interaction between the fα tail, MIA, and the β-propeller domains of a FAP57 homodimer.

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