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5ADX

CryoEM structure of dynactin complex at 4.0 angstrom resolution

Replaces:  5AFT
Summary for 5ADX
Entry DOI10.2210/pdb5adx/pdb
EMDB information2856 2857
DescriptorACTIN RELATED PROTEIN 1, DYNACTIN 5, DYNACTIN SUBUNIT 6, ... (17 entities in total)
Functional Keywordsstructural protein, dynein co-factor, actin-like filament, cellular cargo transport
Biological sourceSUS SCROFA (PIG)
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Cellular locationCytoplasm, cytoskeleton: Q6QAQ1
Total number of polymer chains27
Total formula weight805390.81
Authors
Zhang, K.,Urnavicius, L.,Diamant, A.G.,Motz, C.,Schlage, M.A.,Yu, M.,Patel, N.A.,Robinson, C.V.,Carter, A.P. (deposition date: 2015-08-24, release date: 2015-12-30, Last modification date: 2024-05-08)
Primary citationUrnavicius, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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