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Title | ATP-driven remodeling of the linker domain in the dynein motor. |
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Journal, issue, pages | Structure, Vol. 20, Issue 10, Page 1670-1680, Year 2012 |
Publish date | Oct 10, 2012 |
Authors | Anthony J Roberts / Bara Malkova / Matt L Walker / Hitoshi Sakakibara / Naoki Numata / Takahide Kon / Reiko Ohkura / Thomas A Edwards / Peter J Knight / Kazuo Sutoh / Kazuhiro Oiwa / Stan A Burgess / |
PubMed Abstract | Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are ...Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped enzymes, but how they harness this architecture to produce movement is poorly understood. Here, we have used cryo-EM to determine 3D maps of native flagellar dynein-c and a cytoplasmic dynein motor domain in different nucleotide states. The structures show key sites of conformational change within the AAA+ ring and a large rearrangement of the "linker" domain, involving a hinge near its middle. Analysis of a mutant in which the linker "undocks" from the ring indicates that linker remodeling requires energy that is supplied by interactions with the AAA+ modules. Fitting the dynein-c structures into flagellar tomograms suggests how this mechanism could drive sliding between microtubules, and also has implications for cytoplasmic cargo transport. |
External links | Structure / PubMed:22863569 / PubMed Central |
Methods | EM (single particle) |
Resolution | 19.0 - 22.0 Å |
Structure data | EMDB-2155: EMDB-2156: |
Source |
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