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Open data
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Basic information
| Entry | Database: PDB / ID: 30dr | ||||||||||||
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| Title | Dynein-Dynactin-RAB11FIP3 complex - composite | ||||||||||||
Components |
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Keywords | MOTOR PROTEIN / dynein / dynactin / adaptors / RAB11FIP3 / R11F3 / FIP3 | ||||||||||||
| Function / homology | Function and homology information: / regulation of protein localization to centrosome / protein localization to cleavage furrow / : / Advanced glycosylation endproduct receptor signaling / postsynaptic recycling endosome membrane / regulation of endocytic recycling / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling ...: / regulation of protein localization to centrosome / protein localization to cleavage furrow / : / Advanced glycosylation endproduct receptor signaling / postsynaptic recycling endosome membrane / regulation of endocytic recycling / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / RHOF GTPase cycle / Formation of the canonical BAF (cBAF) complex / Formation of the polybromo-BAF (pBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / GBP-mediated host defense / sterol sensor activity / Platelet degranulation / visual behavior / Gap junction degradation / Formation of annular gap junctions / UCH proteinases / dynactin complex / centriolar subdistal appendage / Clathrin-mediated endocytosis / negative regulation of adiponectin secretion / centriole-centriole cohesion / positive regulation of mitotic cytokinetic process / positive regulation of neuromuscular junction development / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Recruitment of mitotic centrosome proteins and complexes / microtubule anchoring at centrosome / F-actin capping protein complex / intraciliary retrograde transport / WASH complex / Regulation of CDH1 Function / Formation of the dystrophin-glycoprotein complex (DGC) / regulation of cilium assembly / lysosome to ER cholesterol transport / dynein light chain binding / transport along microtubule / ventral spinal cord development / dynein heavy chain binding / VxPx cargo-targeting to cilium / retromer complex / cytoskeleton-dependent cytokinesis / dynein complex / regulation of vesicle-mediated transport / microtubule plus-end / mitotic nuclear membrane disassembly / Intraflagellar transport / positive regulation of microtubule nucleation / protein localization to cilium / cellular response to cytochalasin B / positive regulation of cilium assembly / positive regulation of intracellular transport / positive regulation of spindle assembly / regulation of transepithelial transport / regulation of metaphase plate congression / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / protein localization to adherens junction / non-motile cilium assembly / barbed-end actin filament capping / endocytic recycling / Golgi to plasma membrane protein transport / establishment of spindle localization / dense body / Neutrophil degranulation / Tat protein binding / motor behavior / postsynaptic actin cytoskeleton / positive regulation of mitotic cell cycle spindle assembly checkpoint / apical protein localization / neuron cellular homeostasis / retrograde transport, endosome to Golgi / retrograde axonal transport / adherens junction assembly / COPI-independent Golgi-to-ER retrograde traffic / neuromuscular process / minus-end-directed microtubule motor activity / P-body assembly / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / microtubule associated complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / dynein light intermediate chain binding / cytoplasmic dynein complex / MHC class II antigen presentation / nuclear migration / Recruitment of NuMA to mitotic centrosomes Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human)![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 10 Å | ||||||||||||
Authors | d'Amico, E.A. / Carter, A.P. | ||||||||||||
| Funding support | United Kingdom, 3items
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Citation | Journal: To Be PublishedTitle: Molecular basis of dynein adaptor recognition Authors: d'Amico, E.A. / Chaaban, S. / Abid Ali, F. / Michalski, L. / Carter, A.P. | ||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 30dr.cif.gz | 2.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb30dr.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 30dr.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/0d/30dr ftp://data.pdbj.org/pub/pdb/validation_reports/0d/30dr | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 57643MC ![]() 57636 ![]() 57637 ![]() 57639 ![]() 57641 ![]() 57648 M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 9 types, 23 molecules 12ABCDEFGIHJKLUghopstwz
| #1: Protein | Mass: 86452.945 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RAB11FIP3, ARFO1, KIAA0665 / Production host: ![]() #2: Protein | Mass: 42670.688 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | | Mass: 46250.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 33059.848 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | | Mass: 30669.768 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | | Mass: 20703.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 68514.203 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1I2, DNCI2, DNCIC2 / Production host: ![]() #16: Protein | Mass: 10934.576 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNLRB1, BITH, DNCL2A, DNLC2A, ROBLD1, HSPC162 / Production host: ![]() |
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-Dynactin subunit ... , 5 types, 11 molecules MNPQVORSTWY
| #7: Protein | Mass: 44732.469 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 21192.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 142015.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | | Mass: 20150.533 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 52920.434 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Cytoplasmic dynein 1 ... , 2 types, 7 molecules efmnjqr
| #13: Protein | Mass: 533055.125 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325 / Production host: ![]() #15: Protein | Mass: 54173.156 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1LI2, DNCLI2, LIC2 / Production host: ![]() |
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-Details
| Has protein modification | N |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: dynein-dynactin-RAB11FIP3 / Type: COMPLEX Entity ID: #1-#6, #8, #11, #16, #9, #7, #15, #13-#14, #10, #12 Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.2 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 10 Å / Resolution method: OTHER / Num. of particles: 159084 / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Source name: PDB / Type: experimental model | ||||||||||||||||||||||||
| Refinement | Highest resolution: 10 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)

United Kingdom, 3items
Citation

PDBj



























FIELD EMISSION GUN