ATP-Driven Remodeling of the Linker Domain in the Dynein Motor
| Autor: | Kazuo Sutoh, Reiko Ohkura, Takahide Kon, Hitoshi Sakakibara, Stan A. Burgess, Thomas A. Edwards, Matt L. Walker, Peter J. Knight, Naoki Numata, Bara Malkova, Kazuhiro Oiwa, Anthony J. Roberts |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Axoneme Conformational change Dynein Protozoan Proteins macromolecular substances Biology Microtubules 03 medical and health sciences Adenosine Triphosphate Protein structure Microtubule Structural Biology Dictyostelium Protein Structure Quaternary Cytoskeleton Molecular Biology Plant Proteins 030304 developmental biology 0303 health sciences Microscopy Video Cryoelectron Microscopy 030302 biochemistry & molecular biology Axonemal Dyneins Protein Structure Tertiary Cell biology Adenosine Diphosphate Structural Homology Protein Cytoplasm Linker Chlamydomonas reinhardtii Protein Binding |
| Zdroj: | Structure. 20(10):1670-1680 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2012.07.003 |
| Popis: | Summary 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. |
| Databáze: | OpenAIRE |
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