EMD-2861
Electron cryo-microscopy of dynein/dynactin/GFP-BICD2N complex
EMD-2861
Single-particle11.8 Å
Deposition: 26/01/2015Map released: 15/04/2015
Last modified: 22/04/2015
Sample Organism:
Homo sapiens,
Sus scrofa domesticus,
Mus musculus
Sample: Cryo-EM structure of dynein tail/dynactin/GFP-BICD2N (subset of particles)
Deposition Authors: Urnavicius L, Zhang K
,
Diamant AG,
Motz C,
Schlager MA,
Yu M,
Patel NA,
Robinson CV ,
Carter AP
Sample: Cryo-EM structure of dynein tail/dynactin/GFP-BICD2N (subset of particles)
Deposition Authors: Urnavicius L, Zhang K
,
Diamant AG,
Motz C,
Schlager MA,
Yu M,
Patel NA,
Robinson CV ,
Carter AP
The structure of the dynactin complex and its interaction with dynein.
Urnavicius L,
Zhang K ,
Diamant AG,
Motz C,
Schlager MA,
Yu M,
Patel NA,
Robinson CV ,
Carter AP
(2015) Science , 347 , 1441 - 1446
,
Diamant AG,
Motz C,
Schlager MA,
Yu M,
Patel NA,
Robinson CV ,
Carter AP
(2015) Science , 347 , 1441 - 1446
Abstract:
Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components.
Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components.