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7JTS

Stalk of radial spoke 1 attached with doublet microtubule from Chlamydomonas reinhardtii

Summary for 7JTS
Entry DOI10.2210/pdb7jts/pdb
EMDB information22475 22480
DescriptorRadial spoke protein 3, Dynein 8 kDa light chain, flagellar outer arm, FAP207, ... (5 entities in total)
Functional Keywordscilia, native, complex, microtubule, mechanoregulation, structural protein
Biological sourceChlamydomonas reinhardtii
More
Total number of polymer chains13
Total formula weight318181.15
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: 2020-08-18, release date: 2020-12-16, Last modification date: 2024-03-06)
Primary citationGui, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.1 Å)
Structure validation

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