6F1T

Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Cryo-EM shows how dynactin recruits two dyneins for faster movement.

Urnavicius, L.Lau, C.K.Elshenawy, M.M.Morales-Rios, E.Motz, C.Yildiz, A.Carter, A.P.

(2018) Nature 554: 202-206

  • DOI: https://doi.org/10.1038/nature25462
  • Primary Citation of Related Structures:  
    5OWO, 6F1T, 6F1U, 6F1V, 6F1Y, 6F1Z, 6F38, 6F3A

  • PubMed Abstract: 

    Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.


  • 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
ARP1 actin related protein 1 homolog A
A, B, C, D, E
A, B, C, D, E, F, G, I
376Sus scrofaMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Actin, cytoplasmic 1375Sus scrofaMutation(s): 0 
UniProt
Find proteins for Q6QAQ1 (Sus scrofa)
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Actin related protein 10 homolog390Sus scrofaMutation(s): 0 
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Capping protein (Actin filament) muscle Z-line, alpha 1286Sus scrofaMutation(s): 0 
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
F-actin capping protein beta subunit272Sus scrofaMutation(s): 0 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 2589Sus scrofaMutation(s): 0 
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 2618Sus scrofaMutation(s): 0 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 3
O, P
65Sus scrofaMutation(s): 0 
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 2
Q, R
87Sus scrofaMutation(s): 0 
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin 6S [auth U]190Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin subunit 5T [auth V]182Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR-1U [auth X]389Mus musculusMutation(s): 0 
Gene Names: Bicdl1Bicdr1Ccdc64
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IMPC:  MGI:1922915
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 4V [auth Y]263Sus scrofaMutation(s): 0 
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 1W [auth Z]52Sus scrofaMutation(s): 0 
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin subunit 2X [auth a]66Sus scrofaMutation(s): 0 
UniProt
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin subunit 2Y [auth b]89Sus scrofaMutation(s): 0 
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Entity ID: 17
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin subunit 2Z [auth c]50Sus scrofaMutation(s): 0 
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Entity ID: 18
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin subunit 2AA [auth d]26Sus scrofaMutation(s): 0 
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Entity ID: 19
MoleculeChains Sequence LengthOrganismDetailsImage
Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein 1 heavy chain 1,Dynein Heavy Chain,Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein 1 heavy chain 1,Dynein Heavy Chain,Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein 1 heavy chain 1BA [auth e],
CA [auth f],
JA [auth m],
KA [auth n]
1,053Homo sapiensMutation(s): 0 
Gene Names: DYNC1H1DHC1DNCH1DNCLDNECLDYHCKIAA0325
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PHAROS:  Q14204
GTEx:  ENSG00000197102 
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Entity ID: 20
MoleculeChains Sequence LengthOrganismDetailsImage
Cytoplasmic dynein 1 intermediate chain 2DA [auth g],
EA [auth h],
LA [auth o],
MA [auth p]
612Homo sapiensMutation(s): 0 
Gene Names: DYNC1I2DNCI2DNCIC2
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GTEx:  ENSG00000077380 
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Entity ID: 21
MoleculeChains Sequence LengthOrganismDetailsImage
Cytoplasmic dynein 1 light intermediate chain 2FA [auth i],
GA [auth j],
NA [auth q],
OA [auth r]
492Homo sapiensMutation(s): 0 
Gene Names: DYNC1LI2DNCLI2LIC2
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GTEx:  ENSG00000135720 
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Entity ID: 22
MoleculeChains Sequence LengthOrganismDetailsImage
Dynein light chain roadblock-type 1HA [auth k],
IA [auth l],
PA [auth s],
QA [auth t]
96Homo sapiensMutation(s): 0 
Gene Names: DYNLRB1BITHDNCL2ADNLC2AROBLD1HSPC162
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GTEx:  ENSG00000125971 
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Entity ID: 23
MoleculeChains Sequence LengthOrganismDetailsImage
BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICD family-like cargo adapter 1RA [auth x]392Mus musculusMutation(s): 0 
Gene Names: Bicdl1Bicdr1Ccdc64
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IMPC:  MGI:1922915
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Entity ID: 24
MoleculeChains Sequence LengthOrganismDetailsImage
Dynactin Subunit 1SA [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

Download Ideal Coordinates CCD File 
AB [auth H]ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
ADP
Query on ADP

Download Ideal Coordinates CCD File 
BB [auth I]
CB [auth J]
TA [auth A]
UA [auth B]
VA [auth C]
BB [auth I],
CB [auth J],
TA [auth A],
UA [auth B],
VA [auth C],
WA [auth D],
XA [auth E],
YA [auth F],
ZA [auth G]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION
MODEL REFINEMENTPHENIX

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (United Kingdom)United KingdomMC_UP_A025_1011
Wellcome TrustUnited KingdomWT100387

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-17
    Type: Initial release
  • Version 1.1: 2018-01-31
    Changes: Database references, Refinement description
  • Version 1.2: 2018-02-21
    Changes: Database references
  • Version 1.3: 2019-12-11
    Changes: Other