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7JRJ

Chlamydomonas reinhardtii radial spoke head and neck (recombinant)

Summary for 7JRJ
Entry DOI10.2210/pdb7jrj/pdb
Related7JR9
EMDB information22444 22446
DescriptorRadial spoke protein 10, Flagellar radial spoke protein 6, Flagellar radial spoke protein 10, ... (14 entities in total)
Functional Keywordscilia, radial spoke, mechano-regulation, structural protein
Biological sourceChlamydomonas reinhardtii
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Total number of polymer chains15
Total formula weight518327.66
Authors
Grossman-Haham, I.,Coudray, N.,Yu, Z.,Wang, F.,Zhang, N.,Bhabha, G.,Vale, R.D. (deposition date: 2020-08-12, release date: 2020-12-16, Last modification date: 2024-10-23)
Primary citationGrossman-Haham, I.,Coudray, N.,Yu, Z.,Wang, F.,Zhang, N.,Bhabha, G.,Vale, R.D.
Structure of the radial spoke head and insights into its role in mechanoregulation of ciliary beating.
Nat.Struct.Mol.Biol., 28:20-28, 2021
Cited by
PubMed Abstract: Motile cilia power cell locomotion and drive extracellular fluid flow by propagating bending waves from their base to tip. The coordinated bending of cilia requires mechanoregulation by the radial spoke (RS) protein complexes and the microtubule central pair (CP). Despite their importance for ciliary motility across eukaryotes, the molecular function of the RSs is unknown. Here, we reconstituted the Chlamydomonas reinhardtii RS head that abuts the CP and determined its structure using single-particle cryo-EM to 3.1-Å resolution, revealing a flat, negatively charged surface supported by a rigid core of tightly intertwined proteins. Mutations in this core, corresponding to those involved in human ciliopathies, compromised the stability of the recombinant complex, providing a molecular basis for disease. Partially reversing the negative charge on the RS surface impaired motility in C. reinhardtii. We propose that the RS-head architecture is well-suited for mechanoregulation of ciliary beating through physical collisions with the CP.
PubMed: 33318704
DOI: 10.1038/s41594-020-00519-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.03 Å)
Structure validation

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