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- EMDB-3707: Locally refined human cytoplasmic dynein-1 tail bound to dynactin... -

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Basic information

Entry
Database: EMDB / ID: EMD-3707
TitleLocally refined human cytoplasmic dynein-1 tail bound to dynactin and an N-terminal construct of BICD2
Map dataFocused refinement of the dynein tail improved its density near the LIC binding site.
Sample
  • Complex: Locally refined human cytoplasmic dynein-1 tail bound to dynactin and an N-terminal construct of BICD2
Function / homology
Function and homology information


kinetochore => GO:0000776 / retrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / dense body / Neutrophil degranulation / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / barbed-end actin filament capping / coronary vasculature development ...kinetochore => GO:0000776 / retrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / dense body / Neutrophil degranulation / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / barbed-end actin filament capping / coronary vasculature development / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / MHC class II antigen presentation / COPI-mediated anterograde transport / aorta development / ventricular septum development / dynein complex binding / endoplasmic reticulum to Golgi vesicle-mediated transport / microtubule-based process / COPI-mediated anterograde transport / axon cytoplasm / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / mitotic spindle organization / kinetochore / antigen processing and presentation of exogenous peptide antigen via MHC class II / actin binding / cell cortex / actin cytoskeleton organization / nuclear membrane / cytoskeleton / focal adhesion / centrosome / nucleoplasm / ATP binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Dynamitin / Dynamitin / Dynactin subunit 6 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. ...Dynamitin / Dynamitin / Dynactin subunit 6 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / Hexapeptide repeat / Bacterial transferase hexapeptide (six repeats) / Trimeric LpxA-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain
Similarity search - Domain/homology
Dynactin / Dynactin subunit 2 / Dynactin / Uncharacterized protein / F-actin-capping protein subunit alpha-1 / Dynactin subunit 6 / F-actin-capping protein subunit beta / Alpha-centractin / Actin-related protein 10 / Actin, cytoplasmic 2 / Dynactin subunit 5
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 12.0 Å
AuthorsZhang K / Foster HE / Carter AP
CitationJournal: Cell / Year: 2017
Title: Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated.
Authors: Kai Zhang / Helen E Foster / Arnaud Rondelet / Samuel E Lacey / Nadia Bahi-Buisson / Alexander W Bird / Andrew P Carter /
Abstract: Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves ...Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves poorly on its own or how it is activated by dynactin. Here, we present a cryoelectron microscopy structure of the complete 1.4-megadalton human dynein-1 complex in an inhibited state known as the phi-particle. We reveal the 3D structure of the cargo binding dynein tail and show how self-dimerization of the motor domains locks them in a conformation with low microtubule affinity. Disrupting motor dimerization with structure-based mutagenesis drives dynein-1 into an open form with higher affinity for both microtubules and dynactin. We find the open form is also inhibited for movement and that dynactin relieves this by reorienting the motor domains to interact correctly with microtubules. Our model explains how dynactin binding to the dynein-1 tail directly stimulates its motor activity.
History
DepositionMay 5, 2017-
Header (metadata) releaseMay 31, 2017-
Map releaseJun 28, 2017-
UpdateJul 12, 2017-
Current statusJul 12, 2017Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.06
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.06
  • Imaged by UCSF Chimera
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Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_3707.png

Downloads & links

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Map

FileDownload / File: emd_3707.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFocused refinement of the dynein tail improved its density near the LIC binding site.
Voxel sizeX=Y=Z: 2.68 Å
Density
Contour LevelBy AUTHOR: 0.06 / Movie #1: 0.06
Minimum - Maximum-0.114667855 - 0.3030043
Average (Standard dev.)0.0012422398 (±0.011147462)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions160160160
Spacing160160160
CellA=B=C: 428.80002 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.682.682.68
M x/y/z160160160
origin x/y/z0.0000.0000.000
length x/y/z428.800428.800428.800
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS160160160
D min/max/mean-0.1150.3030.001

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Supplemental data

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Sample components

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Entire : Locally refined human cytoplasmic dynein-1 tail bound to dynactin...

EntireName: Locally refined human cytoplasmic dynein-1 tail bound to dynactin and an N-terminal construct of BICD2
Components
  • Complex: Locally refined human cytoplasmic dynein-1 tail bound to dynactin and an N-terminal construct of BICD2

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Supramolecule #1: Locally refined human cytoplasmic dynein-1 tail bound to dynactin...

SupramoleculeName: Locally refined human cytoplasmic dynein-1 tail bound to dynactin and an N-terminal construct of BICD2
type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 1.6 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionDetails: Particles were selected from phase-flipped micrographs
CTF correctionSoftware - Name: Gctf (ver. 1.06)
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 12.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 78671
FSC plot (resolution estimation)

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