+Open data
-Basic information
Entry | Database: PDB / ID: 7rsi | |||||||||||||||
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Title | The cryo-EM map of KIF18A bound to KIFBP | |||||||||||||||
Components |
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Keywords | MOTOR PROTEIN / kinesin regualtion protein | |||||||||||||||
Function / homology | Function and homology information tubulin-dependent ATPase activity / mitotic spindle astral microtubule / mitotic spindle midzone / central nervous system projection neuron axonogenesis / kinetochore microtubule / male meiotic nuclear division / microtubule plus-end binding / Kinesins / plus-end-directed microtubule motor activity / microtubule depolymerization ...tubulin-dependent ATPase activity / mitotic spindle astral microtubule / mitotic spindle midzone / central nervous system projection neuron axonogenesis / kinetochore microtubule / male meiotic nuclear division / microtubule plus-end binding / Kinesins / plus-end-directed microtubule motor activity / microtubule depolymerization / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / mitotic metaphase chromosome alignment / mitochondrial transport / seminiferous tubule development / microtubule-based movement / mitotic sister chromatid segregation / kinesin binding / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / regulation of microtubule cytoskeleton organization / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / ruffle / Resolution of Sister Chromatid Cohesion / neuron projection maintenance / MHC class II antigen presentation / caveola / cellular response to estradiol stimulus / RHO GTPases Activate Formins / kinetochore / microtubule cytoskeleton organization / Separation of Sister Chromatids / microtubule cytoskeleton / protein transport / actin binding / microtubule binding / in utero embryonic development / cytoskeleton / centrosome / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.9 Å | |||||||||||||||
Authors | Tan, Z. / Solon, A.L. / Schutt, K.L. / Jepsen, L. / Haynes, S.E. / Nesvizhskii, A.I. / Sept, D. / Stumpff, J. / Ohi, R. / Cianfrocco, M.A. | |||||||||||||||
Funding support | United States, 4items
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Citation | Journal: Sci Adv / Year: 2021 Title: Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding. Authors: April L Solon / Zhenyu Tan / Katherine L Schutt / Lauren Jepsen / Sarah E Haynes / Alexey I Nesvizhskii / David Sept / Jason Stumpff / Ryoma Ohi / Michael A Cianfrocco / Abstract: Kinesins are regulated in space and time to ensure activation only in the presence of cargo. Kinesin-binding protein (KIFBP), which is mutated in Goldberg-Shprintzen syndrome, binds to and inhibits ...Kinesins are regulated in space and time to ensure activation only in the presence of cargo. Kinesin-binding protein (KIFBP), which is mutated in Goldberg-Shprintzen syndrome, binds to and inhibits the catalytic motor heads of 8 of 45 kinesin superfamily members, but the mechanism remains poorly defined. Here, we used cryo–electron microscopy and cross-linking mass spectrometry to determine high-resolution structures of KIFBP alone and in complex with two mitotic kinesins, revealing structural remodeling of kinesin by KIFBP. We find that KIFBP remodels kinesin motors and blocks microtubule binding (i) via allosteric changes to kinesin and (ii) by sterically blocking access to the microtubule. We identified two regions of KIFBP necessary for kinesin binding and cellular regulation during mitosis. Together, this work further elucidates the molecular mechanism of KIFBP-mediated kinesin inhibition and supports a model in which structural rearrangement of kinesin motor domains by KIFBP abrogates motor protein activity. | |||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7rsi.cif.gz | 266.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7rsi.ent.gz | 212.5 KB | Display | PDB format |
PDBx/mmJSON format | 7rsi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rs/7rsi ftp://data.pdbj.org/pub/pdb/validation_reports/rs/7rsi | HTTPS FTP |
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-Related structure data
Related structure data | 24672MC 7rsqC 7rypC 7ryqC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 71913.945 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIFBP, KBP, KIAA1279, KIF1BP Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: Q96EK5 |
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#2: Protein | Mass: 39560.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIF18A, OK/SW-cl.108 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: Q8NI77 |
#3: Chemical | ChemComp-MG / |
#4: Chemical | ChemComp-ADP / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: KIFBP:KIF18A complex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7.7 |
Specimen | Conc.: 0.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: GOLD / Grid type: UltrAuFoil R1.2/1.3 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
-Electron microscopy imaging
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
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Microscopy | Model: FEI TALOS ARCTICA |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: OTHER |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy |
Image recording | Electron dose: 60 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 4.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 54801 / Symmetry type: POINT |
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |