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7K5B

Structure of outer-arm dynein bound to microtubule doublet in microtubule binding state 2 (MTBS-2)

This is a non-PDB format compatible entry.
Summary for 7K5B
Entry DOI10.2210/pdb7k5b/pdb
EMDB information22677 22679 22840
DescriptorDynein heavy chain, outer arm protein, Dynein light chain, Dynein light chain tctex-type 1 protein, ... (21 entities in total)
Functional Keywordsthree head, outer dynein arms, microtubule binding, motor protein
Biological sourceTetrahymena thermophila
More
Total number of polymer chains18
Total formula weight1828819.94
Authors
Rao, Q.,Zhang, K. (deposition date: 2020-09-16, release date: 2021-09-29, Last modification date: 2024-11-20)
Primary citationRao, Q.,Han, L.,Wang, Y.,Chai, P.,Kuo, Y.W.,Yang, R.,Hu, F.,Yang, Y.,Howard, J.,Zhang, K.
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism.
Nat.Struct.Mol.Biol., 28:799-810, 2021
Cited by
PubMed Abstract: Thousands of outer-arm dyneins (OADs) are arrayed in the axoneme to drive a rhythmic ciliary beat. Coordination among multiple OADs is essential for generating mechanical forces to bend microtubule doublets (MTDs). Using electron microscopy, we determined high-resolution structures of Tetrahymena thermophila OAD arrays bound to MTDs in two different states. OAD preferentially binds to MTD protofilaments with a pattern resembling the native tracks for its distinct microtubule-binding domains. Upon MTD binding, free OADs are induced to adopt a stable parallel conformation, primed for array formation. Extensive tail-to-head (TTH) interactions between OADs are observed, which need to be broken for ATP turnover by the dynein motor. We propose that OADs in an array sequentially hydrolyze ATP to slide the MTDs. ATP hydrolysis in turn relaxes the TTH interfaces to effect free nucleotide cycles of downstream OADs. These findings lead to a model explaining how conformational changes in the axoneme produce coordinated action of dyneins.
PubMed: 34556869
DOI: 10.1038/s41594-021-00656-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

237735

数据于2025-06-18公开中

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