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. 2023 Apr 13;42(12):e112466. doi: 10.15252/embj.2022112466

Figure 5. Pre‐PS conformation of the ODA.

Figure 5

  • A
    Cross section of one MTD in the pre‐PS conformation.
  • B–D
    Tomographic slices for the γ (B), β (C) and α HC (D), respectively. The MTBD of the γ and α dynein is indicated with a white arrowhead.
  • E, F
    Two views of the overall structure of ODA in the pre‐PS conformation with the pre‐PS model (γ PDB‐4RH7, β & α PDB‐6ZYW and modified tail of PDB‐7MOQ) fitted.
  • G–L
    Enlarged view of individual dyneins in surface‐rendered representations with the pre‐PS model juxtaposed. The linker‐to‐tail connections are indicated by black arrowheads. The cytoplasmic pre‐PS dynein PDB‐4RH7 (Schmidt et al2015) shows that the γ linker is in a bend conformation and that the MTBD is contacting the adjacent B‐tubule. The stalk is visible for the β‐dynein (C, H, I, K, L). If the stalk had an extended conformation like in the cytoplasmic PDB‐4RH7 conformation, the MTBD of the β‐HC would penetrate into the adjacent B‐tubule (H, I). This is due to the dynein head position, which is too close to the adjacent B‐tubule. The β stalk rather appears to be in a bend conformation which is much more similar to the conformation adapted in the Shulin–ODA complex (Mali et al2021) (K and L). The head of the α‐Shulin–ODA (J) is in agreement to the tomographic map. The linker and the MTBD are located in tomographic density.
  • M
    20 Å resolution map of the post‐PS tail complex (calculated from PDB‐7MOQ) shown in a pre‐PS tomographic map.
  • N
    20 Å resolution map of the real‐space‐refined pre‐PS model overlaid on post‐PS tail to highlight the changes.
  • O
    20 Å resolution map of the real‐space‐refined pre‐PS model fitted in the pre‐PS tomographic map.