|Entry||Database: EMDB / ID: 2609|
|Title||KIF14 Motor Domain Microtubule complex|
|Map data||kinesin KIF14 mtor domain micerotubule complex|
|Sample||Kinesin KIF14 motor domain microtubule complex:|
Kinesin KIF14 motor domain / Tubulin
|Keywords||Kinesin / Micotubule / Tubulin / KIF14 / Kinesin-3|
|Source||Mus musculus (house mouse) / Bos taurus (cattle)|
|Method||helical reconstruction / cryo EM / 15.5 Å resolution|
|Authors||Arora K / Talje L / Asenjo AB / Andersen P / Atchia K / Joshi M / Sosa H / Allingham JS / Kwok BH|
|Citation||Journal: J. Mol. Biol. / Year: 2014|
Title: KIF14 binds tightly to microtubules and adopts a rigor-like conformation.
Authors: Kritica Arora / Lama Talje / Ana B Asenjo / Parker Andersen / Kaleem Atchia / Monika Joshi / Hernando Sosa / John S Allingham / Benjamin H Kwok
Abstract: The mitotic kinesin motor protein KIF14 is essential for cytokinesis during cell division and has been implicated in cerebral development and a variety of human cancers. Here we show that the mouse ...The mitotic kinesin motor protein KIF14 is essential for cytokinesis during cell division and has been implicated in cerebral development and a variety of human cancers. Here we show that the mouse KIF14 motor domain binds tightly to microtubules and does not display typical nucleotide-dependent changes in this affinity. It also has robust ATPase activity but very slow motility. A crystal structure of the ADP-bound form of the KIF14 motor domain reveals a dramatically opened ATP-binding pocket, as if ready to exchange its bound ADP for Mg·ATP. In this state, the central β-sheet is twisted ~10° beyond the maximal amount observed in other kinesins. This configuration has only been seen in the nucleotide-free states of myosins-known as the "rigor-like" state. Fitting of this atomic model to electron density maps from cryo-electron microscopy indicates a distinct binding configuration of the motor domain to microtubules. We postulate that these properties of KIF14 are well suited for stabilizing midbody microtubules during cytokinesis.
|Date||Deposition: Mar 20, 2014 / Header (metadata) release: Apr 2, 2014 / Map release: Nov 19, 2014 / Last update: Nov 19, 2014|
|Structure viewer||EM map: |
Downloads & links
|File||emd_2609.map.gz (map file in CCP4 format, 941 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 2 Å|
CCP4 map header:
-Entire Kinesin KIF14 motor domain microtubule complex
|Entire||Name: Kinesin KIF14 motor domain microtubule complex / Number of components: 2|
-Component #1: protein, Kinesin KIF14 motor domain
|Protein||Name: Kinesin KIF14 motor domain / Recombinant expression: Yes|
|Source||Species: Mus musculus (house mouse)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
-Component #2: protein, Tubulin
|Protein||Name: Tubulin / Recombinant expression: No|
|Source||Species: Bos taurus (cattle)|
|Specimen||Specimen state: helical array / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Hand: RIGHT HANDED / Delta z: 5.40237 Å / Delta phi: 168.08788 deg.|
|Vitrification||Instrument: FEI VITROBOT MARK I / Cryogen name: ETHANE / Humidity: 100 %|
-Electron microscopy imaging
|Imaging||Microscope: FEI TECNAI 20 / Date: Nov 25, 2013|
|Electron gun||Electron source: LAB6 / Accelerating voltage: 120 kV / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD / Defocus: 1000 - 2600 nm|
|Specimen Holder||Model: GATAN LIQUID NITROGEN|
|Camera||Detector: TVIPS TEMCAM-F415 (4k x 4k)|
|Image acquisition||Number of digital images: 30|
|Processing||Method: helical reconstruction|
Details: Initial reference map obtained by Fourier-Bessel reconstruction as implemented in SUPRIM & PHOELIX Single particle alignment, 3D reconstruction and refinement done using IHRSR, SPIDER and custom routines.
|3D reconstruction||Software: SUPRIM, PHOELIX, IHRSR, SPIDER, CTFFIND3, CUSTOM, (emglue.py)|
CTF correction: Each Particle / Resolution: 15.5 Å / Resolution method: FSC 0.143, gold-standard
-Atomic model buiding
|Modeling #1||Software: Chimera / Refinement protocol: rigid body / Refinement space: REAL|
Details: The 2 domains (tubulin heterodimer and KIF14 motor domain) were separately fitted. 1 nm resolution density maps of the atomic models were fitted within the cryo-em map using the global fit option of the fitmap command of the UCSF-CHIMERA program.
Input PDB model: 4OZQ
|Modeling #2||Refinement protocol: rigid body / Refinement space: REAL|
Input PDB model: 1JFF
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