7JTK

Radial spoke 1 isolated from Chlamydomonas reinhardtii

Summary for 7JTK

• Entry DOI: 10.2210/pdb7jtk/pdb
• EMDB information: 22475 22480
• Descriptor: Flagellar radial spoke protein 1, Flagellar radial spoke protein 11, Flagellar radial spoke protein 12, ... (20 entities in total)
• Functional Keywords: cilia, native, complex, mechanoregulation, structural protein
• Biological source: Chlamydomonas reinhardtii; More
• Total number of polymer chains: 39
• Total formula weight: 1572377.94

Authors

Gui, M.,Ma, M.,Sze-Tu, E.,Wang, X.,Koh, F.,Zhong, E.,Berger, B.,Davis, J.,Dutcher, S.,Zhang, R.,Brown, A. (deposition date: 2020-08-17, release date: 2020-12-16, Last modification date: 2024-11-13)

Primary citation

Gui, M.,Ma, M.,Sze-Tu, E.,Wang, X.,Koh, F.,Zhong, E.D.,Berger, B.,Davis, J.H.,Dutcher, S.K.,Zhang, R.,Brown, A.
Structures of radial spokes and associated complexes important for ciliary motility.
Nat.Struct.Mol.Biol., 28:29-37, 2021

PubMed Abstract: In motile cilia, a mechanoregulatory network is responsible for converting the action of thousands of dynein motors bound to doublet microtubules into a single propulsive waveform. Here, we use two complementary cryo-EM strategies to determine structures of the major mechanoregulators that bind ciliary doublet microtubules in Chlamydomonas reinhardtii. We determine structures of isolated radial spoke RS1 and the microtubule-bound RS1, RS2 and the nexin-dynein regulatory complex (N-DRC). From these structures, we identify and build atomic models for 30 proteins, including 23 radial-spoke subunits. We reveal how mechanoregulatory complexes dock to doublet microtubules with regular 96-nm periodicity and communicate with one another. Additionally, we observe a direct and dynamically coupled association between RS2 and the dynein motor inner dynein arm subform c (IDAc), providing a molecular basis for the control of motor activity by mechanical signals. These structures advance our understanding of the role of mechanoregulation in defining the ciliary waveform.

PubMed: 33318703
DOI: 10.1038/s41594-020-00530-0

Experimental method

ELECTRON MICROSCOPY (3.2 Å)