3J68

Structural mechanism of the dynein powerstroke (pre-powerstroke state)

Summary for 3J68

• Entry DOI: 10.2210/pdb3j68/pdb
• Related: 3J67 4AKI
• EMDB information: 5757 5758
• Descriptor: Dynein motor domain (1 entity in total)
• Functional Keywords: motor protein
• Biological source: Strongylocentrotus purpuratus (purple sea urchin)
• Total number of polymer chains: 1
• Total formula weight: 262122.23

Authors

Lin, J.,Okada, K.,Raytchev, M.,Smith, M.C.,Nicastro, D. (deposition date: 2013-12-23, release date: 2014-04-23, Last modification date: 2024-02-21)

Primary citation

Lin, J.,Okada, K.,Raytchev, M.,Smith, M.C.,Nicastro, D.
Structural mechanism of the dynein power stroke.
Nat.Cell Biol., 16:479-485, 2014

PubMed Abstract: Dyneins are large microtubule motor proteins required for mitosis, intracellular transport and ciliary and flagellar motility. They generate force through a power-stroke mechanism, which is an ATP-consuming cycle of pre- and post-power-stroke conformational changes that cause relative motion between different dynein domains. However, key structural details of dynein's force generation remain elusive. Here, using cryo-electron tomography of intact, active (that is, beating), rapidly frozen sea urchin sperm flagella, we determined the in situ three-dimensional structures of all domains of both pre- and post-power-stroke dynein, including the previously unresolved linker and stalk of pre-power-stroke dynein. Our results reveal that the rotation of the head relative to the linker is the key action in dynein movement, and that there are at least two distinct pre-power-stroke conformations: pre-I (microtubule-detached) and pre-II (microtubule-bound). We provide three-dimensional reconstructions of native dyneins in three conformational states, in situ, allowing us to propose a molecular model of the structural cycle underlying dynein movement.

PubMed: 24727830
DOI: 10.1038/ncb2939

Experimental method

ELECTRON MICROSCOPY (30 Å)