|Entry||Database: EMDB / ID: 9637|
|Title||5R-MAP4, kinesin-1, and microtubule complex|
|Source||Bos taurus (cattle)|
|Method||helical reconstruction / cryo EM / 7.29 Å resolution|
|Authors||Shigematsu H / Imasaki T / Doki C / Sumi T / Aoki M / Uchikubo-Kamo T / Sakamoto A / Tokuraku K / Shirouzu M / Nitta R|
|Citation||Journal: J. Cell Biol. / Year: 2018|
Title: Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs.
Authors: Hideki Shigematsu / Tsuyoshi Imasaki / Chihiro Doki / Takuya Sumi / Mari Aoki / Tomomi Uchikubo-Kamo / Ayako Sakamoto / Kiyotaka Tokuraku / Mikako Shirouzu / Ryo Nitta
Abstract: The Tau family microtubule-associated proteins (MAPs) promote microtubule stabilization and regulate microtubule-based motility. They share the C-terminal microtubule-binding domain, which includes ...The Tau family microtubule-associated proteins (MAPs) promote microtubule stabilization and regulate microtubule-based motility. They share the C-terminal microtubule-binding domain, which includes three to five tubulin-binding repeats. Different numbers of repeats formed by alternative splicing have distinct effects on the activities of these proteins, and the distribution of these variants regulates fundamental physiological phenomena in cells. In this study, using cryo-EM, we visualized the MAP4 microtubule complex with the molecular motor kinesin-1. MAP4 bound to the C-terminal domains of tubulins along the protofilaments stabilizes the longitudinal contacts of the microtubule. The strongest bond of MAP4 was found around the intertubulin-dimer interface such that MAP4 coexists on the microtubule with kinesin-1 bound to the intratubulin-dimer interface as well. MAP4, consisting of five repeats, further folds and accumulates above the intertubulin-dimer interface, interfering with kinesin-1 movement. Therefore, these cryo-EM studies reveal new insight into the structural basis of microtubule stabilization and inhibition of kinesin motility by the Tau family MAPs.
|Date||Deposition: Aug 28, 2018 / Header (metadata) release: Oct 10, 2018 / Map release: Oct 10, 2018 / Last update: Oct 17, 2018|
|Structure viewer||EM map: |
Downloads & links
|File||emd_9637.map.gz (map file in CCP4 format, 15437 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.284 Å|
CCP4 map header:
-Entire Microtubule-Kinesin-1-5R-MAP4 complex
|Entire||Name: Microtubule-Kinesin-1-5R-MAP4 complex / Number of components: 1|
-Component #1: protein, Microtubule-Kinesin-1-5R-MAP4 complex
|Protein||Name: Microtubule-Kinesin-1-5R-MAP4 complex / Recombinant expression: No|
|Source||Species: Bos taurus (cattle)|
|Source (engineered)||Expression System: Escherichia coli (E. coli) / Vector: pET21d / Strain: BL21(DE3)pLysS|
|Specimen||Specimen state: filament / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 8.7 Å / Delta phi: -25.76 deg.|
|Sample solution||Buffer solution: 100 mM PIPES-KOH at pH 6.8, 1 mM MgCl2, 1 mM EGTA|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 300 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI ARCTICA|
Details: Alignment procedure by FEI User Interface Software. Not determined the residual tilt value.
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 55 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 78000.0 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1500.0 - 2500.0 nm|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Processing||Method: helical reconstruction|
|3D reconstruction||Resolution: 7.29 Å / Resolution method: FSC 0.143 CUT-OFF|
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