|Entry||Database: EMDB / ID: 9385|
|Title||The central pair complex of sea urchin (Strongylocentrotus purpuratus) sperm resolved by cryo-electron tomography and sub-tomogram averaging|
|Map data||The central pair complex of sea urchin (Strongylocentrotus purpuratus) sperm resolved by cryo-electron tomography and sub-tomogram averaging|
|Sample||The central pair complex/apparatus (2167 repeats) averaged from 41 Strongylocentrotus sea urchin sperms:|
|Source||Strongylocentrotus purpuratus (purple sea urchin)|
|Method||subtomogram averaging / cryo EM / 35 Å resolution|
|Authors||Carbajal-Gonzalez BI / Heuser T / Fu X / Lin J / Smith BW / Mitchell DR / Fu G / Nicastro D|
|Citation||Journal: Cytoskeleton (Hoboken) / Year: 2013|
Title: Conserved structural motifs in the central pair complex of eukaryotic flagella.
Authors: Blanca I Carbajal-González / Thomas Heuser / Xiaofeng Fu / Jianfeng Lin / Brandon W Smith / David R Mitchell / Daniela Nicastro
Abstract: Cilia and flagella are conserved hair-like appendages of eukaryotic cells that function as sensing and motility generating organelles. Motility is driven by thousands of axonemal dyneins that require ...Cilia and flagella are conserved hair-like appendages of eukaryotic cells that function as sensing and motility generating organelles. Motility is driven by thousands of axonemal dyneins that require precise regulation. One essential motility regulator is the central pair complex (CPC) and many CPC defects cause paralysis of cilia/flagella. Several human diseases, such as immotile cilia syndrome, show CPC abnormalities, but little is known about the detailed three-dimensional (3D) structure and function of the CPC. The CPC is located in the center of typical [9+2] cilia/flagella and is composed of two singlet microtubules (MTs), each with a set of associated projections that extend toward the surrounding nine doublet MTs. Using cryo-electron tomography coupled with subtomogram averaging, we visualized and compared the 3D structures of the CPC in both the green alga Chlamydomonas and the sea urchin Strongylocentrotus at the highest resolution published to date. Despite the evolutionary distance between these species, their CPCs exhibit remarkable structural conservation. We identified several new projections, including those that form the elusive sheath, and show that the bridge has a more complex architecture than previously thought. Organism-specific differences include the presence of MT inner proteins in Chlamydomonas, but not Strongylocentrotus, and different overall outlines of the highly connected projection network, which forms a round-shaped cylinder in algae, but is more oval in sea urchin. These differences could be adaptations to the mechanical requirements of the rotating CPC in Chlamydomonas, compared to the Strongylocentrotus CPC which has a fixed orientation.
|Date||Deposition: Jan 2, 2019 / Header (metadata) release: Jan 16, 2019 / Map release: Jan 16, 2019 / Last update: Jan 16, 2019|
|Structure viewer||EM map: |
Downloads & links
|File||emd_9385.map.gz (map file in CCP4 format, 4001 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 9.856 Å|
CCP4 map header:
-Entire The central pair complex/apparatus (2167 repeats) averaged from 4...
|Entire||Name: The central pair complex/apparatus (2167 repeats) averaged from 41 Strongylocentrotus sea urchin sperms|
Number of components: 1
-Component #1: cellular-component, The central pair complex/apparatus (2167 repe...
|Cellular-component||Name: The central pair complex/apparatus (2167 repeats) averaged from 41 Strongylocentrotus sea urchin sperms|
Recombinant expression: No
|Source||Species: Strongylocentrotus purpuratus (purple sea urchin)|
|Source (natural)||Organelle: sperm / Location in cell: tail of sperm|
|Specimen||Specimen state: cell / Method: cryo EM|
|Sample solution||Buffer solution: artificial sea water / pH: 7.4|
|Vitrification||Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Temperature: 298 K|
Details: back-side blotting for 1.5-2.5 seconds before plunging.
-Electron microscopy imaging
Model: Tecnai F30 / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI F30|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 1.5 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 13500.0 X (calibrated) / Imaging mode: BRIGHT FIELD / Energy filter: GIF 2000|
|Specimen Holder||Model: GATAN LIQUID NITROGEN|
|Camera||Detector: GATAN ULTRASCAN 1000 (2k x 2k)|
|Processing||Method: subtomogram averaging / Applied symmetry: C1 (asymmetric) / Number of subtomograms: 2167|
|3D reconstruction||Algorithm: BACK PROJECTION / Software: IMOD / Resolution: 35 Å / Resolution method: FSC 0.5 CUT-OFF|
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