ATP-driven remodeling of the linker domain in the dynein motor.
Structure
; 20(10): 1670-80, 2012 Oct 10.
Article
en En
| MEDLINE
| ID: mdl-22863569
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.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Adenosina Trifosfato
/
Chlamydomonas reinhardtii
/
Dictyostelium
/
Dineínas Axonemales
Idioma:
En
Revista:
Structure
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2012
Tipo del documento:
Article
País de afiliación:
Reino Unido