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- PDB-7som: Ciliary C2 central pair apparatus isolated from Chlamydomonas rei... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7som | ||||||
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Title | Ciliary C2 central pair apparatus isolated from Chlamydomonas reinhardtii | ||||||
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![]() | STRUCTURAL PROTEIN / cilia / microtubule | ||||||
Function / homology | ![]() axonemal central apparatus / axonemal central pair / axonemal doublet microtubule / positive regulation of cilium-dependent cell motility / sperm axoneme assembly / regulation of cilium beat frequency involved in ciliary motility / establishment of protein localization to organelle / cilium movement / axoneme assembly / axonemal microtubule ...axonemal central apparatus / axonemal central pair / axonemal doublet microtubule / positive regulation of cilium-dependent cell motility / sperm axoneme assembly / regulation of cilium beat frequency involved in ciliary motility / establishment of protein localization to organelle / cilium movement / axoneme assembly / axonemal microtubule / motile cilium / microtubule associated complex / regulation of cytoskeleton organization / axoneme / cilium assembly / sperm flagellum / ciliary basal body / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / microtubule cytoskeleton organization / mitotic cell cycle / microtubule binding / microtubule / transcription coactivator activity / hydrolase activity / GTPase activity / calcium ion binding / regulation of DNA-templated transcription / GTP binding / extracellular exosome / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||
![]() | Gui, M. / Wang, X. / Dutcher, S.K. / Brown, A. / Zhang, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Ciliary central apparatus structure reveals mechanisms of microtubule patterning. Authors: Miao Gui / Xiangli Wang / Susan K Dutcher / Alan Brown / Rui Zhang / ![]() Abstract: A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules ...A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules are patterned asymmetrically with large protein complexes that repeat every 16 or 32 nm. The composition of these projections and the mechanisms that establish asymmetry and longitudinal periodicity are unknown. Here, by determining cryo-EM structures of the CA microtubules, we identify 48 different CA-associated proteins, which in turn reveal mechanisms for asymmetric and periodic protein binding to microtubules. We identify arc-MIPs, a novel class of microtubule inner protein, that bind laterally across protofilaments and remodel tubulin structure and lattice contacts. The binding mechanisms utilized by CA proteins may be generalizable to other microtubule-associated proteins. These structures establish a foundation to elucidate the contributions of individual CA proteins to ciliary motility and ciliopathies. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 13.2 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 9.6 MB | Display | ![]() |
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Full document | ![]() | 9.7 MB | Display | |
Data in XML | ![]() | 1.1 MB | Display | |
Data in CIF | ![]() | 2.1 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 25361MC ![]() 7sqcC 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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Components
-Protein , 16 types, 198 molecules AAACAEAGAIAKBABCBEBGBIBKCCCECGCICKDCDEDGDIDKEAECEEEGEIEKFAFC...
#1: Protein | Mass: 49665.809 Da / Num. of mol.: 74 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 49638.008 Da / Num. of mol.: 74 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | Mass: 64880.324 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Protein | Mass: 22262.674 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 81430.711 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #6: Protein | Mass: 57734.598 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #7: Protein | Mass: 46261.570 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #8: Protein | Mass: 10089.324 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #9: Protein | Mass: 22193.566 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #10: Protein | Mass: 65929.133 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #11: Protein | Mass: 10336.616 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #12: Protein | Mass: 233221.547 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #13: Protein | Mass: 111116.258 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #14: Protein | Mass: 102141.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #15: Protein | Mass: 23511.406 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #17: Protein | Mass: 6571.091 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Protein/peptide , 2 types, 2 molecules A1A3
#16: Protein/peptide | Mass: 4103.049 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#18: Protein/peptide | Mass: 4017.944 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 3 types, 222 molecules ![](data/chem/img/GDP.gif)
![](data/chem/img/GTP.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/GTP.gif)
![](data/chem/img/MG.gif)
#19: Chemical | ChemComp-GDP / #20: Chemical | ChemComp-GTP / #21: Chemical | ChemComp-MG / |
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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: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: C2 central pair apparatus complex / Type: COMPLEX / Entity ID: #1-#2, #13-#18, #3, #11-#12, #7-#10, #4-#6 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: C-flat-1.2/1.3 |
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: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 39.6 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
3D reconstruction | Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 104806 / Symmetry type: POINT |