5AFR

N-terminal fragment of dynein heavy chain

Summary for 5AFR

• Entry DOI: 10.2210/pdb5afr/pdb
• Descriptor: DYNEIN HEAVY CHAIN, CYTOPLASMIC (1 entity in total)
• Functional Keywords: motor protein, dynein, tail, heavy chain
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cytoplasm, cytoskeleton : P36022
• Total number of polymer chains: 2
• Total formula weight: 128758.32

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: 2015-01-23, release date: 2015-02-18, Last modification date: 2024-11-13)

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

X-RAY DIFFRACTION (5 Å)