+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-24536 | |||||||||
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Title | MTBS-1 of KLP1 on C2 | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Chlamydomonas reinhardtii (plant) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 10.44 Å | |||||||||
Authors | Han L / Zhang K | |||||||||
Funding support | United States, 1 items
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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 |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_24536.map.gz | 31.5 MB | EMDB map data format | |
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Header (meta data) | emd-24536-v30.xml emd-24536.xml | 15.3 KB 15.3 KB | Display Display | EMDB header |
Images | emd_24536.png | 58.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-24536 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-24536 | HTTPS FTP |
-Validation report
Summary document | emd_24536_validation.pdf.gz | 410.8 KB | Display | EMDB validaton report |
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Full document | emd_24536_full_validation.pdf.gz | 410.3 KB | Display | |
Data in XML | emd_24536_validation.xml.gz | 6.6 KB | Display | |
Data in CIF | emd_24536_validation.cif.gz | 7.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24536 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24536 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_24536.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 4.32249 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : C1 microtubule and its associated projection of central pair
Entire | Name: C1 microtubule and its associated projection of central pair |
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Components |
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-Supramolecule #1: C1 microtubule and its associated projection of central pair
Supramolecule | Name: C1 microtubule and its associated projection of central pair type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#52 |
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Source (natural) | Organism: Chlamydomonas reinhardtii (plant) / Strain: cc124 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Average electron dose: 38.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Calibrated magnification: 65000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 0.0025 µm / Nominal defocus min: 0.0012 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 10.44 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 40834 |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |