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Open data
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Basic information
Entry | Database: PDB / ID: 7n6g | ||||||
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Title | C1 of central pair | ||||||
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![]() | STRUCTURAL PROTEIN / central pair | ||||||
Function / homology | ![]() axonemal central pair projection / : / axonemal central apparatus / axonemal central apparatus assembly / organelle / establishment of meiotic spindle localization / cilium movement involved in cell motility / cilium movement / guanylate kinase activity / axoneme assembly ...axonemal central pair projection / : / axonemal central apparatus / axonemal central apparatus assembly / organelle / establishment of meiotic spindle localization / cilium movement involved in cell motility / cilium movement / guanylate kinase activity / axoneme assembly / calcium-dependent cysteine-type endopeptidase activity / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / adenylate kinase / adenylate kinase activity / MLL3/4 complex / Set1C/COMPASS complex / motile cilium / spindle organization / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / axoneme / chaperone cofactor-dependent protein refolding / cilium assembly / subtelomeric heterochromatin formation / enzyme regulator activity / protein folding chaperone / heat shock protein binding / tubulin binding / glycolytic process / electron transport chain / ATP-dependent protein folding chaperone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cilium / structural constituent of cytoskeleton / spindle pole / microtubule cytoskeleton organization / microtubule cytoskeleton / mitotic cell cycle / chromosome, telomeric region / protein refolding / microtubule binding / microtubule / calmodulin binding / hydrolase activity / negative regulation of cell population proliferation / GTPase activity / nucleotide binding / calcium ion binding / GTP binding / magnesium ion binding / ATP hydrolysis activity / proteolysis / ATP binding / membrane / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | ||||||
![]() | Han, L. / Zhang, K. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of an active central apparatus. Authors: Long Han / Qinhui Rao / Renbin Yang / Yue Wang / Pengxin Chai / Yong Xiong / Kai Zhang / ![]() Abstract: Accurately regulated ciliary beating in time and space is critical for diverse cellular activities, which impact the survival and development of nearly all eukaryotic species. An essential beating ...Accurately regulated ciliary beating in time and space is critical for diverse cellular activities, which impact the survival and development of nearly all eukaryotic species. An essential beating regulator is the conserved central apparatus (CA) of motile cilia, composed of a pair of microtubules (C1 and C2) associated with hundreds of protein subunits per repeating unit. It is largely unclear how the CA plays its regulatory roles in ciliary motility. Here, we present high-resolution structures of Chlamydomonas reinhardtii CA by cryo-electron microscopy (cryo-EM) and its dynamic conformational behavior at multiple scales. The structures show how functionally related projection proteins of CA are clustered onto a spring-shaped scaffold of armadillo-repeat proteins, facilitated by elongated rachis-like proteins. The two halves of the CA are brought together by elastic chain-like bridge proteins to achieve coordinated activities. We captured an array of kinesin-like protein (KLP1) in two different stepping states, which are actively correlated with beating wave propagation of cilia. These findings establish a structural framework for understanding the role of the CA in cilia. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 17.6 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 8.4 MB | Display | ![]() |
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Full document | ![]() | 8.8 MB | Display | |
Data in XML | ![]() | 2.2 MB | Display | |
Data in CIF | ![]() | 3.5 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 24207MC ![]() 7n61C 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
+Protein , 49 types, 260 molecules 0A0B0C0D0E0F0G0L0M0N0O0P0Q0R0S0T0U0V0X0Y0Z1A1B1C0H0J0W0I0K1D...
-Protein/peptide , 3 types, 4 molecules 2M2O3A3B
#19: Protein/peptide | Mass: 1549.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#21: Protein/peptide | Mass: 4017.944 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#27: Protein/peptide | Mass: 3081.790 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 2 types, 104 molecules ![](data/chem/img/GDP.gif)
![](data/chem/img/GTP.gif)
![](data/chem/img/GTP.gif)
#53: Chemical | ChemComp-GDP / #54: Chemical | ChemComp-GTP / |
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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: C1 microtubule and its associated projection of central pair Type: COMPLEX / Entity ID: #1-#52 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
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: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1200 nm |
Image recording | Electron dose: 38.6 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
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Processing
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 190727 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 103.11 Å2 | ||||||||||||||||||||||||
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