5AFU

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


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The Structure of the Dynactin Complex and its Interaction with Dynein.

Urnavicius, L.Zhang, K.Diamant, A.G.Motz, C.Schlager, M.A.Yu, M.Patel, N.A.Robinson, C.V.Carter, A.P.

(2015) Science 347: 1441

  • DOI: https://doi.org/10.1126/science.aaa4080
  • Primary Citation of Related Structures:  
    5ADX, 5AFR, 5AFU

  • 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.


  • Organizational Affiliation

    Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DYNEIN TAILA [auth 1]361Sus scrofaMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
DYNEIN TAILB [auth 2]359Sus scrofaMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
DYNEIN TAILC [auth 3],
D [auth 4]
350Sus scrofaMutation(s): 0 
UniProt
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UniProt GroupA0A0J9X2A1
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
DYNEIN TAILE [auth 5],
F [auth 6]
275Sus scrofaMutation(s): 0 
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTIN370Sus scrofaMutation(s): 0 
UniProt
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UniProt GroupF2Z5G5
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
ACTIN, CYTOPLASMIC 1N [auth H]370Sus scrofaMutation(s): 0 
UniProt
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UniProt GroupQ6QAQ1
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINP [auth J]379Sus scrofaMutation(s): 0 
UniProt
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UniProt GroupI3LHK5
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1Q [auth K]275Sus scrofaMutation(s): 0 
UniProt
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UniProt GroupA0PFK5
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT IIR [auth L]270Sus scrofaMutation(s): 0 
UniProt
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UniProt GroupD2JYW4
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINS [auth M]587Sus scrofaMutation(s): 0 
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTIN 6T [auth N]616Sus scrofaMutation(s): 0 
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINU [auth O],
V [auth P]
65Sus scrofaMutation(s): 0 
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINW [auth Q],
X [auth R]
87Sus scrofaMutation(s): 0 
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINY [auth U]168Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINZ [auth V]165Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
F-ACTIN-CAPPING PROTEIN SUBUNIT BETAAA [auth Y]243Sus scrofaMutation(s): 0 
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Entity ID: 17
MoleculeChains Sequence LengthOrganismDetailsImage
F-ACTIN-CAPPING PROTEIN SUBUNIT BETABA [auth Z]52Sus scrofaMutation(s): 0 
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Entity ID: 18
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINCA [auth a]48Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 19
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINDA [auth b]71Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 20
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINEA [auth c]31Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 21
MoleculeChains Sequence LengthOrganismDetailsImage
DYNACTINFA [auth d]20Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 22
MoleculeChains Sequence LengthOrganismDetailsImage
F-ACTIN-CAPPING PROTEIN SUBUNIT BETAGA [auth z]53Sus scrofaMutation(s): 0 
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Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ATP
Query on ATP

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OA [auth H]ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
ADP
Query on ADP

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HA [auth A]
IA [auth B]
JA [auth C]
KA [auth D]
LA [auth E]
HA [auth A],
IA [auth B],
JA [auth C],
KA [auth D],
LA [auth E],
MA [auth F],
NA [auth G],
PA [auth I],
QA [auth J]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-03-11
    Type: Initial release
  • Version 1.1: 2015-04-08
    Changes: Database references