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- EMDB-10060: Cryo-EM structure of the human inner arm dynein DNAH7 microtubule... -

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Basic information

Entry
Database: EMDB / ID: EMD-10060
TitleCryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules
Map data
SampleDNAH7 microtubule binding domain bound to microtubules
  • DNAH7
  • tubulin
  • Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7, axonemal,Cytoplasmic dynein 1 heavy chain 1
  • Tubulin alpha-1B chain
  • Tubulin beta chain
  • (ligand) x 4
Function / homology
Function and homology information


Separation of Sister Chromatids / Regulation of PLK1 Activity at G2/M Transition / Mitotic Prometaphase / COPI-independent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / Neutrophil degranulation / RHO GTPases Activate Formins / Anchoring of the basal body to the plasma membrane / Recruitment of NuMA to mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome ...Separation of Sister Chromatids / Regulation of PLK1 Activity at G2/M Transition / Mitotic Prometaphase / COPI-independent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / Neutrophil degranulation / RHO GTPases Activate Formins / Anchoring of the basal body to the plasma membrane / Recruitment of NuMA to mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Loss of Nlp from mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) / Resolution of Sister Chromatid Cohesion / Separation of Sister Chromatids / MHC class II antigen presentation / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / HSP90 chaperone cycle for steroid hormone receptors (SHR) / Kinesins / Carboxyterminal post-translational modifications of tubulin / The role of GTSE1 in G2/M progression after G2 checkpoint / Mitotic Prometaphase / COPI-independent Golgi-to-ER retrograde traffic / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / RHO GTPases Activate Formins / RHO GTPases activate IQGAPs / Intraflagellar transport / Cilium Assembly / Recruitment of NuMA to mitotic centrosomes / Hedgehog 'off' state / AURKA Activation by TPX2 / Resolution of Sister Chromatid Cohesion / axonemal dynein complex / cilium-dependent cell motility / inner dynein arm assembly / inner dynein arm / cilium movement / positive regulation of intracellular transport / positive regulation of spindle assembly / minus-end-directed vesicle transport along microtubule / establishment of spindle localization / dynein light chain binding / manchette / ATP-dependent microtubule motor activity, minus-end-directed / cytoplasmic mRNA processing body assembly / dynein light intermediate chain binding / regulation of metaphase plate congression / cytoplasmic dynein complex / dynein complex / retrograde axonal transport / nuclear migration / regulation of mitotic spindle organization / dynein intermediate chain binding / stress granule assembly / cytoplasmic microtubule organization / microtubule motor activity / cytoplasmic microtubule / microtubule-based movement / axon cytoplasm / microtubule-based process / cilium / filopodium / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / positive regulation of cold-induced thermogenesis / nuclear envelope / cell cortex / mitotic cell cycle / microtubule / GTPase activity / centrosome / cell division / axon / GTP binding / neuronal cell body / calcium ion binding / ATP binding / cytosol / cytoplasm
Dynein heavy chain / Tubulin/FtsZ, C-terminal domain superfamily / Tubulin C-terminal domain / Dynein heavy chain region D6 P-loop domain / Tubulin/FtsZ family, GTPase domain / Dynein heavy chain, domain 2, C-terminal / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain AAA lid domain / Dynein heavy chain 3, AAA+ lid domain ...Dynein heavy chain / Tubulin/FtsZ, C-terminal domain superfamily / Tubulin C-terminal domain / Dynein heavy chain region D6 P-loop domain / Tubulin/FtsZ family, GTPase domain / Dynein heavy chain, domain 2, C-terminal / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain AAA lid domain / Dynein heavy chain 3, AAA+ lid domain / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain, C-terminal domain / Tubulin/FtsZ, GTPase domain superfamily / Dynein heavy chain, N-terminal region 2 / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / P-loop containing nucleoside triphosphate hydrolase / Dynein heavy chain, coiled coil stalk / Dynein heavy chain, AAA module D4 / Tubulin, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / EF-Hand 1, calcium-binding site / Tubulin, conserved site / Beta tubulin, autoregulation binding site / Dynein heavy chain, N-terminal region 1 / Hydrolytic ATP binding site of dynein motor region / Dynein heavy chain, domain-1 / Microtubule-binding stalk of dynein motor / Tubulin-beta mRNA autoregulation signal. / Tubulin subunits alpha, beta, and gamma signature. / Dynein heavy chain C-terminal domain / Dynein heavy chain AAA lid domain / AAA+ lid domain / Dynein heavy chain AAA lid domain / ATP-binding dynein motor region / P-loop containing dynein motor region D4 / Dynein heavy chain, domain-2 / Tubulin/FtsZ, C-terminal / Dynein heavy chain region D6 P-loop domain / AAA+ ATPase domain / Tubulin/FtsZ, GTPase domain / Beta tubulin / Alpha tubulin / EF-hand domain / Tubulin
Tubulin beta chain / Tubulin alpha-1B chain / Dynein heavy chain 7, axonemal / Cytoplasmic dynein 1 heavy chain 1
Biological speciesHomo sapiens (human) / Sus scrofa (pig) / Mus musculus (house mouse) / Pig (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.5 Å
AuthorsLacey SE / He S / Scheres SHW / Carter AP
CitationJournal: Elife / Year: 2019
Title: Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.
Authors: Samuel E Lacey / Shaoda He / Sjors Hw Scheres / Andrew P Carter /
Abstract: Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain ...Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule.
Validation ReportPDB-ID: 6rza

SummaryFull reportAbout validation report
DateDeposition: Jun 13, 2019 / Header (metadata) release: Jul 10, 2019 / Map release: Jul 10, 2019 / Update: Jul 17, 2019

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.022
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.022
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: : PDB-6rza
  • Surface level: 0.022
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic models: PDB-6rza
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_10060.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 512 pix.
= 555.52 Å
1.09 Å/pix.
x 512 pix.
= 555.52 Å
1.09 Å/pix.
x 512 pix.
= 555.52 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.085 Å
Density
Contour LevelBy AUTHOR: 0.022 / Movie #1: 0.022
Minimum - Maximum-0.05202959 - 0.11244631
Average (Standard dev.)0.00064605195 (±0.0057806615)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 555.52 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0851.0851.085
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z555.520555.520555.520
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS512512512
D min/max/mean-0.0660.1250.001

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Supplemental data

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Mask #1

Fileemd_10060_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire DNAH7 microtubule binding domain bound to microtubules

EntireName: DNAH7 microtubule binding domain bound to microtubules
Number of components: 10

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Component #1: protein, DNAH7 microtubule binding domain bound to microtubules

ProteinName: DNAH7 microtubule binding domain bound to microtubules
Recombinant expression: No

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Component #2: protein, DNAH7

ProteinName: DNAH7 / Recombinant expression: No
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #3: protein, tubulin

ProteinName: tubulin / Recombinant expression: No
SourceSpecies: Sus scrofa (pig)

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Component #4: protein, Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7,...

ProteinName: Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7, axonemal,Cytoplasmic dynein 1 heavy chain 1
Details: Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end,Fusion between two proteins. Cytoplasmic dynein 1 sequence from position 1 to 15 DNAH7 sequence from proline at position 16 to proline at position 154 Cytoplasmic dynein 1 sequence again from from 155 to end
Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 18.133164 kDa
SourceSpecies: Mus musculus (house mouse)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #5: protein, Tubulin alpha-1B chain

ProteinName: Tubulin alpha-1B chain / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 48.679051 kDa
SourceSpecies: Pig (pig)
Source (natural)Organ or tissue: Brain

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Component #6: protein, Tubulin beta chain

ProteinName: Tubulin beta chain / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 47.825859 kDa
SourceSpecies: Pig (pig)
Source (natural)Organ or tissue: Brain

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Component #7: ligand, GUANOSINE-5'-TRIPHOSPHATE

LigandName: GUANOSINE-5'-TRIPHOSPHATEGuanosine triphosphate / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 0.52318 kDa

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Component #8: ligand, MAGNESIUM ION

LigandName: MAGNESIUM ION / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 2.430505 MDa

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Component #9: ligand, GUANOSINE-5'-DIPHOSPHATE

LigandName: GUANOSINE-5'-DIPHOSPHATE / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 0.443201 kDa

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Component #10: ligand, TAXOL

LigandName: TAXOLPaclitaxel / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 0.853906 kDa

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Experimental details

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Sample preparation

SpecimenSpecimen state: helical array / Method: cryo EM
Sample solutionpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 67.5 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: OTHER
CameraDetector: FEI FALCON III (4k x 4k)

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Image processing

ProcessingMethod: single particle reconstruction / Number of projections: 41984
3D reconstructionSoftware: RELION / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF

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Atomic model buiding

Modeling #1Refinement protocol: flexible
Output model

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