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- PDB-8v2z: Cryo-EM Structure of Smooth Muscle Gamma Actin (ACTG2) Mutant R257C -
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Open data
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Basic information
Entry | Database: PDB / ID: 8v2z | ||||||
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Title | Cryo-EM Structure of Smooth Muscle Gamma Actin (ACTG2) Mutant R257C | ||||||
![]() | Actin, gamma-enteric smooth muscle | ||||||
![]() | STRUCTURAL PROTEIN / Filament / Actin / Smooth Muscle / CYTOSOLIC PROTEIN | ||||||
Function / homology | ![]() myosin filament / mesenchyme migration / Smooth Muscle Contraction / filopodium / cell periphery / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / lamellipodium / cell body / cytoskeleton / blood microparticle ...myosin filament / mesenchyme migration / Smooth Muscle Contraction / filopodium / cell periphery / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / lamellipodium / cell body / cytoskeleton / blood microparticle / hydrolase activity / positive regulation of gene expression / extracellular space / extracellular exosome / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.72 Å | ||||||
![]() | Palmer, N.J. / Carman, P.J. / Ceron, R.H. / Dominguez, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Smooth Muscle Gamma Actin (ACTG2) Filament Mutant R257C Authors: Ceron, R.H. / Baez-Cruz, F.A. / Palmer, N.J. / Carman, P.J. / Boczkowska, M. / Heuckeroth, R.O. / Ostap, E.M. / Dominguez, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 362.3 KB | Display | ![]() |
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PDB format | ![]() | 295.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 61 KB | Display | |
Data in CIF | ![]() | 90.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 42938MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 41881.762 Da / Num. of mol.: 5 / Mutation: R257C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P63267, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #2: Chemical | ChemComp-ADP / #3: Chemical | ChemComp-MG / 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 |
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Sample preparation
Component | Name: ACTG2 R257C Filament / Type: COMPLEX / Details: ACTG2 filaments, purified from Expi293 cells / Entity ID: #1 / Source: RECOMBINANT | |||||||||||||||||||||||||||||||||||
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Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: NO | |||||||||||||||||||||||||||||||||||
Source (natural) | Organism: ![]() | |||||||||||||||||||||||||||||||||||
Source (recombinant) | Organism: ![]() | |||||||||||||||||||||||||||||||||||
Buffer solution | pH: 8 / Details: Actin F-buffer | |||||||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.168 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: ACTG2 F-actin in the ADP state. R257C mutation | |||||||||||||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K / Details: Blot Force: 0 Blot Time: 2.5 s |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 1021 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: -166.6 ° / Axial rise/subunit: 27.5 Å / Axial symmetry: C1 | |||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.72 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 473627 / Symmetry type: HELICAL | |||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | |||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 8F8P Accession code: 8F8P / Source name: PDB / Type: experimental model | |||||||||||||||||||||||||||||||||||
Refine LS restraints |
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