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- PDB-8ruy: Structure of IFTA and IFTB in Retrograde Intraflagellar transport... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8ruy | |||||||||
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Title | Structure of IFTA and IFTB in Retrograde Intraflagellar transport trains | |||||||||
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![]() | PROTEIN TRANSPORT / Cilia / IFT / train / retrograde | |||||||||
Function / homology | ![]() intraciliary transport particle B binding / intraciliary transport particle / intraciliary transport involved in cilium assembly / intraciliary transport particle B / intraciliary transport particle A / cellular component assembly / outer dynein arm assembly / cilium-dependent cell motility / intraciliary retrograde transport / intraciliary transport ...intraciliary transport particle B binding / intraciliary transport particle / intraciliary transport involved in cilium assembly / intraciliary transport particle B / intraciliary transport particle A / cellular component assembly / outer dynein arm assembly / cilium-dependent cell motility / intraciliary retrograde transport / intraciliary transport / regulation of cilium assembly / axoneme assembly / axonemal microtubule / cilium organization / protein localization to cilium / non-motile cilium assembly / ciliary plasm / non-motile cilium / motile cilium / ciliary membrane / post-transcriptional regulation of gene expression / ciliary base / microtubule organizing center / kinesin binding / axoneme / cilium assembly / beta-tubulin binding / RNA processing / centriole / tubulin binding / regulation of microtubule cytoskeleton organization / regulation of protein stability / apical part of cell / protein transport / microtubule binding / cytoskeleton / protein stabilization / cilium / ciliary basal body / GTPase activity / GTP binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 15.4 Å | |||||||||
![]() | Lacey, S. / Pigino, G. | |||||||||
Funding support | European Union, 2items
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![]() | ![]() Title: Extensive structural rearrangement of intraflagellar transport trains underpins bidirectional cargo transport. Authors: Samuel E Lacey / Andrea Graziadei / Gaia Pigino / ![]() Abstract: Bidirectional transport in cilia is carried out by polymers of the IFTA and IFTB protein complexes, called anterograde and retrograde intraflagellar transport (IFT) trains. Anterograde trains deliver ...Bidirectional transport in cilia is carried out by polymers of the IFTA and IFTB protein complexes, called anterograde and retrograde intraflagellar transport (IFT) trains. Anterograde trains deliver cargoes from the cell to the cilium tip, then convert into retrograde trains for cargo export. We set out to understand how the IFT complexes can perform these two directly opposing roles before and after conversion. We use cryoelectron tomography and in situ cross-linking mass spectrometry to determine the structure of retrograde IFT trains and compare it with the known structure of anterograde trains. The retrograde train is a 2-fold symmetric polymer organized around a central thread of IFTA complexes. We conclude that anterograde-to-retrograde remodeling involves global rearrangements of the IFTA/B complexes and requires complete disassembly of the anterograde train. Finally, we describe how conformational changes to cargo-binding sites facilitate unidirectional cargo transport in a bidirectional system. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 3.3 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 452.9 KB | Display | |
Data in CIF | ![]() | 700 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 19515MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Intraflagellar transport protein ... , 13 types, 17 molecules AJjOPQRSsTiICDEMm
#1: Protein | Mass: 150972.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||||||
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#4: Protein | Mass: 85782.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #8: Protein | | Mass: 71648.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #9: Protein | | Mass: 77186.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #10: Protein | | Mass: 22783.967 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #11: Protein | | Mass: 20380.588 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #12: Protein | Mass: 37976.410 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #13: Protein | | Mass: 21363.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #14: Protein | Mass: 197851.172 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #15: Protein | | Mass: 139382.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #16: Protein | | Mass: 136267.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #17: Protein | | Mass: 152227.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #20: Protein | Mass: 51374.508 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Intraflagellar transport particle protein ... , 2 types, 3 molecules BLl
#2: Protein | Mass: 157426.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#6: Protein | Mass: 15658.664 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein , 5 types, 10 molecules HhKkNnFfGg
#3: Protein | Mass: 50453.184 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 54437.715 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #7: Protein | Mass: 49733.469 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #18: Protein | Mass: 86418.125 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #19: Protein | Mass: 74248.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: CELL / 3D reconstruction method: subtomogram averaging |
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Sample preparation
Component | Name: In situ retrograde intraflagellar transport trains in dhc1b-3 mutant Chlamydomonas reinhardtii cilia Type: CELL Details: Temperature sensitive cells incubated at restrictive temperature (34 degrees C) for 10 hours and plunge frozen on grids. Entity ID: #1-#2, #15-#19, #3, #14, #4-#6, #20, #7-#13 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7 |
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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm |
Image recording | Electron dose: 2.6 e/Å2 / Avg electron dose per subtomogram: 104 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||
3D reconstruction | Resolution: 15.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5896 Details: Composite map, with constituent maps ranging from 15.4 to 28.3 angstrom Symmetry type: POINT | ||||||||||||
EM volume selection | Num. of tomograms: 756 / Num. of volumes extracted: 10455 |