+Open data
-Basic information
Entry | Database: PDB / ID: 7kch | ||||||
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Title | Myosin XI-F-actin complex | ||||||
Components |
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Keywords | CONTRACTILE PROTEIN / myosin / actin / cytoskeleton / motor protein | ||||||
Function / homology | Function and homology information Striated Muscle Contraction / myosin complex / cytoskeletal motor activity / skeletal muscle thin filament assembly / striated muscle thin filament / skeletal muscle fiber development / stress fiber / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement ...Striated Muscle Contraction / myosin complex / cytoskeletal motor activity / skeletal muscle thin filament assembly / striated muscle thin filament / skeletal muscle fiber development / stress fiber / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / actin filament binding / calmodulin binding / hydrolase activity / ATP binding Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) Chara corallina (plant) | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 4.33 Å | ||||||
Authors | Gong, R. / Alushin, G.M. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nat Chem Biol / Year: 2021 Title: Optical control of fast and processive engineered myosins in vitro and in living cells. Authors: Paul V Ruijgrok / Rajarshi P Ghosh / Sasha Zemsky / Muneaki Nakamura / Rui Gong / Lin Ning / Robert Chen / Vipul T Vachharajani / Alexander E Chu / Namrata Anand / Raphael R Eguchi / Po-Ssu ...Authors: Paul V Ruijgrok / Rajarshi P Ghosh / Sasha Zemsky / Muneaki Nakamura / Rui Gong / Lin Ning / Robert Chen / Vipul T Vachharajani / Alexander E Chu / Namrata Anand / Raphael R Eguchi / Po-Ssu Huang / Michael Z Lin / Gregory M Alushin / Jan T Liphardt / Zev Bryant / Abstract: Precision tools for spatiotemporal control of cytoskeletal motor function are needed to dissect fundamental biological processes ranging from intracellular transport to cell migration and division. ...Precision tools for spatiotemporal control of cytoskeletal motor function are needed to dissect fundamental biological processes ranging from intracellular transport to cell migration and division. Direct optical control of motor speed and direction is one promising approach, but it remains a challenge to engineer controllable motors with desirable properties such as the speed and processivity required for transport applications in living cells. Here, we develop engineered myosin motors that combine large optical modulation depths with high velocities, and create processive myosin motors with optically controllable directionality. We characterize the performance of the motors using in vitro motility assays, single-molecule tracking and live-cell imaging. Bidirectional processive motors move efficiently toward the tips of cellular protrusions in the presence of blue light, and can transport molecular cargo in cells. Robust gearshifting myosins will further enable programmable transport in contexts ranging from in vitro active matter reconstitutions to microfabricated systems that harness molecular propulsion. | ||||||
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 | 7kch.cif.gz | 302.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7kch.ent.gz | 229.8 KB | Display | PDB format |
PDBx/mmJSON format | 7kch.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7kch_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 7kch_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 7kch_validation.xml.gz | 73.8 KB | Display | |
Data in CIF | 7kch_validation.cif.gz | 108.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kc/7kch ftp://data.pdbj.org/pub/pdb/validation_reports/kc/7kch | HTTPS FTP |
-Related structure data
Related structure data | 22808MC 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: 42096.953 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: ACTA1, ACTA / Production host: Gallus gallus (chicken) / References: UniProt: P68139 #2: Protein | | Mass: 83015.320 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chara corallina (plant) / Gene: ccm Production host: Spodoptera aff. frugiperda 2 RZ-2014 (butterflies/moths) References: UniProt: Q9SSU1 #3: Chemical | #4: Chemical | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
-Sample preparation
Component | Name: Myosin XI-F-actin complex / Type: COMPLEX / Entity ID: #1-#2 / Source: MULTIPLE SOURCES | |||||||||||||||||||||||||||||||||||
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Molecular weight | Value: 209 kDa/nm / Experimental value: YES | |||||||||||||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7 Details: 10 mM imidazole pH 7.0,50 mM KCl,1mM MgCl2, 1mM EGTA, 0.5 mM DTT, 0.01% NaN3 | |||||||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: C-flat-1.2/1.3 | |||||||||||||||||||||||||||||||||||
Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 293 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: -4000 nm / Nominal defocus min: -1000 nm / Cs: 0 mm / Alignment procedure: ZEMLIN TABLEAU |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 67.12 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: -167.11 ° / Axial rise/subunit: 27.45 Å / Axial symmetry: C1 | ||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 70000 | ||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.33 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 45779 / Algorithm: FOURIER SPACE / Num. of class averages: 23 / Symmetry type: HELICAL |