+Open data
-Basic information
Entry | Database: PDB / ID: 8v30 | ||||||
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Title | Smooth Muscle Gamma Actin (ACTG2) Filament Mutant R40C | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / Filament / Actin / Smooth Muscle / CYTOSOLIC PROTEIN | ||||||
Function / homology | Function and homology information 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 / blood microparticle / cytoskeleton ...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 / blood microparticle / cytoskeleton / hydrolase activity / positive regulation of gene expression / extracellular space / extracellular exosome / ATP binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) synthetic construct (others) | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.54 Å | ||||||
Authors | Palmer, N.J. / Carman, P.J. / Ceron, R.H. / Dominguez, R. | ||||||
Funding support | United States, 1items
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Citation | Journal: To Be Published Title: Molecular Mechanisms of ACTG2 Mutations Linked to Visceral Myopathy 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8v30.cif.gz | 370.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8v30.ent.gz | 303.5 KB | Display | PDB format |
PDBx/mmJSON format | 8v30.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v3/8v30 ftp://data.pdbj.org/pub/pdb/validation_reports/v3/8v30 | HTTPS FTP |
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-Related structure data
Related structure data | 42939MC 8v2oC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 41881.766 Da / Num. of mol.: 5 / Mutation: R40C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: Smooth Muscle / Gene: ACTG2, ACTA3, ACTL3, ACTSG / Cell line (production host): Expi293F / Production host: Homo sapiens (human) References: UniProt: P63267, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #2: Protein/peptide | Type: Peptide-like / Class: Toxin / Mass: 808.899 Da / Num. of mol.: 5 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) / References: BIRD: PRD_002366 #3: Chemical | ChemComp-ADP / #4: 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 |
-Sample preparation
Component | Name: ACTG2 R40C Filament / Type: COMPLEX Details: ACTG2 filaments, purified from Expi293 cells R40C mutation Entity ID: #1 / Source: RECOMBINANT | ||||||||||||||||||||||||||||||||||||||||
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Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: NO | ||||||||||||||||||||||||||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) / Tissue: Smooth Muscle | ||||||||||||||||||||||||||||||||||||||||
Source (recombinant) | Organism: Homo sapiens (human) / Cell: Expi293F | ||||||||||||||||||||||||||||||||||||||||
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. R40C 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 |
-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: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / 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: 4461 |
-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: 2.54 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 3400116 / 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 |