6ZYX

Outer Dynein Arm-Shulin complex - Shulin region from Tetrahymena thermophila

Summary for 6ZYX

• Entry DOI: 10.2210/pdb6zyx/pdb
• EMDB information: 11579
• Descriptor: Dynein heavy chain, outer arm protein, Flagellar outer dynein arm intermediate protein, putative, GUANOSINE-5'-TRIPHOSPHATE, ... (11 entities in total)
• Functional Keywords: cilia, microtubules, motor, complex, motor protein
• Biological source: Tetrahymena thermophila CU428; More
• Total number of polymer chains: 10
• Total formula weight: 905944.11

Authors

Mali, G.R.,Abid Ali, F.,Lau, C.K.,Carter, A.P. (deposition date: 2020-08-03, release date: 2021-01-20, Last modification date: 2024-05-01)

Primary citation

Mali, G.R.,Ali, F.A.,Lau, C.K.,Begum, F.,Boulanger, J.,Howe, J.D.,Chen, Z.A.,Rappsilber, J.,Skehel, M.,Carter, A.P.
Shulin packages axonemal outer dynein arms for ciliary targeting.
Science, 371:910-916, 2021

PubMed Abstract: The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During ciliogenesis, these ~1.8-megadalton complexes are assembled in the cytoplasm and targeted to cilia by an unknown mechanism. Here, we used the ciliate to identify two factors (Q22YU3 and Q22MS1) that bind ODAs in the cytoplasm and are required for ODA delivery to cilia. Q22YU3, which we named Shulin, locked the ODA motor domains into a closed conformation and inhibited motor activity. Cryo-electron microscopy revealed how Shulin stabilized this compact form of ODAs by binding to the dynein tails. Our findings provide a molecular explanation for how newly assembled dyneins are packaged for delivery to the cilia.

PubMed: 33632841
DOI: 10.1126/science.abe0526

Experimental method

ELECTRON MICROSCOPY (4.3 Å)