5AFU

Cryo-EM structure of dynein tail-dynactin-BICD2N complex

Summary for 5AFU

• Entry DOI: 10.2210/pdb5afu/pdb
• EMDB information: 2860
• Descriptor: DYNEIN TAIL, DYNACTIN, DYNACTIN 6, ... (24 entities in total)
• Functional Keywords: dynein, dynactin, bicd2, motor, transport, motor protein
• Biological source: SUS SCROFA (PIG); More
• Cellular location: Cytoplasm, cytoskeleton: 5AFU
• Total number of polymer chains: 33
• Total formula weight: 884750.92

Authors

Urnavicius, L.,Zhang, K.,Diamant, A.G.,Motz, C.,Schlager, M.A.,Yu, M.,Patel, N.A.,Robinson, C.V.,Carter, A.P. (deposition date: 2015-01-26, release date: 2015-03-11, Last modification date: 2024-05-08)

Primary citation

Urnavicius, L.,Zhang, K.,Diamant, A.G.,Motz, C.,Schlager, M.A.,Yu, M.,Patel, N.A.,Robinson, C.V.,Carter, A.P.
The Structure of the Dynactin Complex and its Interaction with Dynein.
Science, 347:1441-, 2015

PubMed 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.

PubMed: 25814576
DOI: 10.1126/SCIENCE.AAA4080

Experimental method

ELECTRON MICROSCOPY (8.2 Å)