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PMID:22863569
| Citation |
Roberts, AJ, Malkova, B, Walker, ML, Sakakibara, H, Numata, N, Kon, T, Ohkura, R, Edwards, TA, Knight, PJ, Sutoh, K, Oiwa, K and Burgess, SA (2012) ATP-driven remodeling of the linker domain in the dynein motor. Structure 20:1670-80 |
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| 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 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. |
| Links |
PubMed PMC3469822 Online version:10.1016/j.str.2012.07.003 |
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| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
part_of |
GO:0030286: dynein complex |
ECO:0000314: direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
| GO:0030286: dynein complex |
ECO:0000314: |
C |
Figure 3.b shows cytoplasmic dynein motors. |
complete | ||||
See also
References
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