|Entry||Database: EMDB / ID: 8532|
|Title||Cryo-EM structure of 16nm repeat ciliary microtubule doublet|
|Map data||16nm repeat map of the doublet from Tetrahymena thermophila|
|Sample||16nm-repeat of microtubule doublet|
|Function/homology||MalF, N-terminal / Maltose transport system permease protein MalF, P2 domain / Maltose transport system, permease protein MalF / ABC transporter, maltose/maltodextrin import, MalK / Maltose/Maltodextrin import ATP-binding protein malK family profile. / maltose transport complex / maltose-transporting ATPase / maltose-transporting ATPase activity / Transport-associated OB, type 2 / Maltose transport system permease protein MalF P2 domain ...MalF, N-terminal / Maltose transport system permease protein MalF, P2 domain / Maltose transport system, permease protein MalF / ABC transporter, maltose/maltodextrin import, MalK / Maltose/Maltodextrin import ATP-binding protein malK family profile. / maltose transport complex / maltose-transporting ATPase / maltose-transporting ATPase activity / Transport-associated OB, type 2 / Maltose transport system permease protein MalF P2 domain / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / ABC transporter integral membrane type-1 domain profile. / TOBE domain / Molybdate/tungstate binding, C-terminal / Binding-protein-dependent transport system inner membrane component / maltose transport / maltodextrin transport / ABC transporters family signature. / ABC transporter, conserved site / activating transcription factor binding / ABC transporter-like / ATP-binding cassette, ABC transporter-type domain profile. / ATP-binding cassette (ABC) transporter complex / ABC transporter / extrinsic component of cytoplasmic side of plasma membrane / AAA+ ATPase domain / cellular response to DNA damage stimulus / integral component of plasma membrane / P-loop containing nucleoside triphosphate hydrolase / membrane / ATP binding / plasma membrane / Maltose transport system permease protein MalF / Maltose transport system permease protein MalG / Maltose/maltodextrin import ATP-binding protein MalK|
Function and homology information
|Source||Tetrahymena thermophila / eukaryote / Tetrahymena|
|Method||single particle reconstruction, at 6.2 Å resolution|
|Authors||Ichikawa M / Liu D / Kastritis PL / Basu K / Bui KH|
|Citation||Journal: Nat Commun / Year: 2017|
Title: Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins.
Authors: Muneyoshi Ichikawa / Dinan Liu / Panagiotis L Kastritis / Kaustuv Basu / Tzu Chin Hsu / Shunkai Yang / Khanh Huy Bui
Abstract: Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the ...Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign α- and β-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule.
|Date||Deposition: Dec 21, 2016 / Header (metadata) release: Jan 18, 2017 / Map release: May 10, 2017 / Last update: Feb 14, 2018|
Downloads & links
|File||emd_8532.map.gz (map file in CCP4 format, 67109 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 2.75 Å|
CCP4 map header:
-Entire 16nm-repeat of microtubule doublet
|Entire||Name: 16nm-repeat of microtubule doublet / Number of components: 1|
-Component #1: cellular-component, 16nm-repeat of microtubule doublet
|Cellular-component||Name: 16nm-repeat of microtubule doublet / Recombinant expression: No|
|Source||Species: Tetrahymena thermophila / eukaryote / Tetrahymena / Strain: SB255|
|Source (natural)||Organelle: cilia / Location in cell: cilia|
|Sample solution||Specimen conc.: 2 mg/ml / pH: 7.4|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 298 K / Humidity: 100 % / Details: Blot force 3 for 5 seconds|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 45 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 59000 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1200 - 3800 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Image acquisition||Number of digital images: 5983|
|Processing||Method: single particle reconstruction / Number of projections: 64116|
|3D reconstruction||Algorithm: BACK PROJECTION / Software: RELION / Resolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF|
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