|Entry||Database: EMDB / ID: EMD-6873|
|Title||A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1)|
|Sample||Axoneme, outer doublet microtubule|
|Biological species||Chlamydomonas reinhardtii (plant)|
|Method||subtomogram averaging / cryo EM / Resolution: 60 Å|
|Authors||Kubo T / Hou Y / Cochran DA / Witman GB / Oda T|
|Citation||Journal: Mol Biol Cell / Year: 2018|
Title: A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1).
Authors: Tomohiro Kubo / Yuqing Hou / Deborah A Cochran / George B Witman / Toshiyuki Oda /
Abstract: Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but ...Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but the molecular mechanism of IDA regulation is poorly understood. Here we show using cryoelectron tomography and biochemical analyses of Chlamydomonas flagella that a conserved protein FAP44 forms a complex that tethers IDA f (I1 dynein) head domains to the A-tubule of the axonemal outer doublet microtubule. In wild-type flagella, IDA f showed little nucleotide-dependent movement except for a tilt in the f β head perpendicular to the microtubule-sliding direction. In the absence of the tether complex, however, addition of ATP and vanadate caused a large conformational change in the IDA f head domains, suggesting that the movement of IDA f is mechanically restricted by the tether complex. Motility defects in flagella missing the tether demonstrates the importance of the IDA f-tether interaction in the regulation of ciliary/flagellar beating.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_6873.map.gz / Format: CCP4 / Size: 9.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
generated in cubic-lattice coordinate
|Voxel size||X=Y=Z: 8 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Axoneme, outer doublet microtubule
|Entire||Name: Axoneme, outer doublet microtubule / Details: FAP43-C-BCCP axoneme labeled with streptavidin / Number of components: 1|
-Component #1: cellular-component, Axoneme, outer doublet microtubule
|Cellular-component||Name: Axoneme, outer doublet microtubule / Details: FAP43-C-BCCP axoneme labeled with streptavidin / Recombinant expression: No|
|Source||Species: Chlamydomonas reinhardtii (plant) / Strain: fap43fap244:FAP43-C-BCCP|
|Source (natural)||Organelle: Flagella|
|Specimen||Specimen state: Filament / Method: cryo EM|
|Sample solution||Specimen conc.: 0.02 mg/mL / pH: 7.2|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277 K / Humidity: 100 % / Details: blot 5.5 sec before plunging.|
-Electron microscopy imaging
|Imaging||Microscope: JEOL 2100F|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 1.6 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: GATAN LIQUID NITROGEN|
|Camera||Detector: TVIPS TEMCAM-F216 (2k x 2k)|
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