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8BWY

In situ outer dynein arm from Chlamydomonas reinhardtii in a pre-power stroke state

Summary for 8BWY
Entry DOI10.2210/pdb8bwy/pdb
EMDB information16304
DescriptorDynein-1-alpha heavy chain, flagellar inner arm I1 complex protein, putative, Dynein light chain, Dynein light chain 2A, ... (20 entities in total)
Functional Keywordsaxoneme, outer dynein arm, pre power stroke, dynein, motor protein
Biological sourceChlamydomonas reinhardtii
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Total number of polymer chains19
Total formula weight1899637.29
Authors
Zimmermann, N.E.L.,Noga, A.,Obbineni, J.M.,Ishikawa, T. (deposition date: 2022-12-07, release date: 2023-05-10, Last modification date: 2024-07-24)
Primary citationZimmermann, N.,Noga, A.,Obbineni, J.M.,Ishikawa, T.
ATP-induced conformational change of axonemal outer dynein arms revealed by cryo-electron tomography.
Embo J., 42:e112466-e112466, 2023
Cited by
PubMed Abstract: Axonemal outer dynein arm (ODA) motors generate force for ciliary beating. We analyzed three states of the ODA during the power stroke cycle using in situ cryo-electron tomography, subtomogram averaging, and classification. These states of force generation depict the prepower stroke, postpower stroke, and intermediate state conformations. Comparison of these conformations to published in vitro atomic structures of cytoplasmic dynein, ODA, and the Shulin-ODA complex revealed differences in the orientation and position of the dynein head. Our analysis shows that in the absence of ATP, all dynein linkers interact with the AAA3/AAA4 domains, indicating that interactions with the adjacent microtubule doublet B-tubule direct dynein orientation. For the prepower stroke conformation, there were changes in the tail that is anchored on the A-tubule. We built models starting with available high-resolution structures to generate a best-fitting model structure for the in situ pre- and postpower stroke ODA conformations, thereby showing that ODA in a complex with Shulin adopts a similar conformation as the active prepower stroke ODA in the axoneme.
PubMed: 37051721
DOI: 10.15252/embj.2022112466
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (38 Å)
Structure validation

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