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Yorodumi- PDB-6rza: Cryo-EM structure of the human inner arm dynein DNAH7 microtubule... -
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-Basic information
Entry | Database: PDB / ID: 6rza | |||||||||
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Title | Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules | |||||||||
Components |
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Keywords | MOTOR PROTEIN / filament / complex | |||||||||
Function / homology | Function and homology information inner dynein arm / inner dynein arm assembly / COPI-independent Golgi-to-ER retrograde traffic / cilium-dependent cell motility / axonemal dynein complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cilium movement involved in cell motility / 9+2 motile cilium / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport ...inner dynein arm / inner dynein arm assembly / COPI-independent Golgi-to-ER retrograde traffic / cilium-dependent cell motility / axonemal dynein complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cilium movement involved in cell motility / 9+2 motile cilium / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / Aggrephagy / positive regulation of intracellular transport / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / cilium movement / regulation of metaphase plate congression / Resolution of Sister Chromatid Cohesion / establishment of spindle localization / positive regulation of spindle assembly / RHO GTPases Activate Formins / Separation of Sister Chromatids / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Regulation of PLK1 Activity at G2/M Transition / manchette / dynein complex / MHC class II antigen presentation / minus-end-directed microtubule motor activity / retrograde axonal transport / dynein light intermediate chain binding / cytoplasmic dynein complex / P-body assembly / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling / The role of GTSE1 in G2/M progression after G2 checkpoint / Aggrephagy / Resolution of Sister Chromatid Cohesion / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Separation of Sister Chromatids / nuclear migration / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / COPI-mediated anterograde transport / microtubule motor activity / dynein intermediate chain binding / cytoplasmic microtubule / cytoplasmic microtubule organization / stress granule assembly / regulation of mitotic spindle organization / axon cytoplasm / Neutrophil degranulation / mitotic spindle organization / filopodium / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / cilium / microtubule cytoskeleton organization / microtubule cytoskeleton / nuclear envelope / mitotic cell cycle / positive regulation of cold-induced thermogenesis / cell cortex / microtubule / cell division / axon / GTPase activity / centrosome / neuronal cell body / calcium ion binding / GTP binding / ATP hydrolysis activity / ATP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) Sus scrofa (pig) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
Authors | Lacey, S.E. / He, S. / Scheres, S.H.W. / Carter, A.P. | |||||||||
Funding support | United Kingdom, 2items
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Citation | Journal: 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. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6rza.cif.gz | 389.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6rza.ent.gz | 312 KB | Display | PDB format |
PDBx/mmJSON format | 6rza.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rz/6rza ftp://data.pdbj.org/pub/pdb/validation_reports/rz/6rza | HTTPS FTP |
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-Related structure data
Related structure data | 10060MC 6rzbC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: MET / Beg label comp-ID: MET / Refine code: _
NCS ensembles :
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-Components
-Protein , 3 types, 5 molecules XACBD
#1: Protein | Mass: 18133.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source 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 ...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 Source: (gene. exp.) Mus musculus (house mouse), (gene. exp.) Homo sapiens (human) Gene: Dync1h1, Dhc1, Dnch1, Dnchc1, Dyhc, DNAH7, KIAA0944 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9JHU4, UniProt: Q8WXX0 | ||
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#2: Protein | Mass: 48679.051 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: Brain / References: UniProt: Q2XVP4 #3: Protein | Mass: 47825.859 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: Brain / References: UniProt: P02554 |
-Non-polymers , 4 types, 8 molecules
#4: Chemical | #5: Chemical | #6: Chemical | #7: Chemical | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component |
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Source (natural) |
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Source (recombinant) | Organism: Escherichia coli (E. coli) | ||||||||||||||||||||||||
Buffer solution | pH: 8 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 67.5 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
-Processing
Software | Name: REFMAC / Version: 5.8.0247 / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 41984 / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | Resolution: 4.5→4.5 Å / Cor.coef. Fo:Fc: 0.582 / SU B: 243.237 / SU ML: 2.563 / ESU R: 2.187 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
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Solvent computation | Solvent model: PARAMETERS FOR MASK CACLULATION | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 206.247 Å2
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Refinement step | Cycle: 1 / Resolution: 5.402→195.3 Å / Total: 14908 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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