7JTS
Stalk of radial spoke 1 attached with doublet microtubule from Chlamydomonas reinhardtii
Summary for 7JTS
Entry DOI | 10.2210/pdb7jts/pdb |
EMDB information | 22475 22480 |
Descriptor | Radial spoke protein 3, Dynein 8 kDa light chain, flagellar outer arm, FAP207, ... (5 entities in total) |
Functional Keywords | cilia, native, complex, microtubule, mechanoregulation, structural protein |
Biological source | Chlamydomonas reinhardtii More |
Total number of polymer chains | 13 |
Total formula weight | 318181.15 |
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 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 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: 33318703DOI: 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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