+Open data
-Basic information
Entry | Database: PDB / ID: 7n6g | ||||||
---|---|---|---|---|---|---|---|
Title | C1 of central pair | ||||||
Components |
| ||||||
Keywords | STRUCTURAL PROTEIN / central pair | ||||||
Function / homology | Function and homology information axonemal central apparatus / axonemal central pair projection / : / axonemal central apparatus assembly / establishment of meiotic spindle localization / sperm axoneme assembly / positive regulation of flagellated sperm motility / sperm principal piece / cilium movement involved in cell motility / epithelial cilium movement involved in extracellular fluid movement ...axonemal central apparatus / axonemal central pair projection / : / axonemal central apparatus assembly / establishment of meiotic spindle localization / sperm axoneme assembly / positive regulation of flagellated sperm motility / sperm principal piece / cilium movement involved in cell motility / epithelial cilium movement involved in extracellular fluid movement / cilium movement / axoneme assembly / guanylate kinase activity / response to odorant / calcium-dependent cysteine-type endopeptidase activity / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / adenylate kinase / adenylate kinase activity / manchette / SRP-dependent cotranslational protein targeting to membrane, translocation / filopodium assembly / MLL3/4 complex / Set1C/COMPASS complex / non-motile cilium / motile cilium / neuron projection extension / spindle organization / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / axoneme / chaperone cofactor-dependent protein refolding / mitochondrial respiratory chain complex I / cilium assembly / subtelomeric heterochromatin formation / enzyme regulator activity / protein folding chaperone / sperm midpiece / heat shock protein binding / tubulin binding / acrosomal vesicle / electron transport chain / glycolytic process / ATP-dependent protein folding chaperone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cilium / structural constituent of cytoskeleton / microtubule cytoskeleton organization / spindle pole / microtubule cytoskeleton / mitotic cell cycle / protein refolding / microtubule binding / microtubule / chromosome, telomeric region / hydrolase activity / calmodulin binding / negative regulation of cell population proliferation / phosphorylation / GTPase activity / calcium ion binding / GTP binding / magnesium ion binding / ATP hydrolysis activity / proteolysis / ATP binding / membrane / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Chlamydomonas reinhardtii (plant) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | ||||||
Authors | Han, L. / Zhang, K. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: Nat Struct Mol Biol / Year: 2022 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7n6g.cif.gz | 17.6 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7n6g.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 7n6g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n6/7n6g ftp://data.pdbj.org/pub/pdb/validation_reports/n6/7n6g | HTTPS FTP |
---|
-Related structure data
Related structure data | 24207MC 7n61C M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-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) Chlamydomonas reinhardtii (plant) / Strain: cc124 |
---|---|
#21: Protein/peptide | Mass: 4017.944 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / Strain: cc124 |
#27: Protein/peptide | Mass: 3081.790 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / Strain: cc124 |
-Non-polymers , 2 types, 104 molecules
#53: Chemical | ChemComp-GDP / #54: Chemical | ChemComp-GTP / |
---|
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: C1 microtubule and its associated projection of central pair Type: COMPLEX / Entity ID: #1-#52 / Source: NATURAL |
---|---|
Source (natural) | Organism: Chlamydomonas reinhardtii (plant) / Strain: cc124 |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / 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) |
-Processing
Software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 | ||||||||||||||||||||||||
Refine LS restraints |
|