+Open data
-Basic information
Entry | Database: PDB / ID: 8wg3 | ||||||
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Title | mouse TMEM63b in LMNG-CHS micelle | ||||||
Components | CSC1-like protein 2,Green fluorescent protein | ||||||
Keywords | LIPID TRANSPORT / Scramblase | ||||||
Function / homology | Function and homology information surfactant secretion / osmolarity-sensing monoatomic cation channel activity / mechanosensitive monoatomic cation channel activity / mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / exocytosis / bioluminescence / generation of precursor metabolites and energy / sensory perception of sound / actin cytoskeleton ...surfactant secretion / osmolarity-sensing monoatomic cation channel activity / mechanosensitive monoatomic cation channel activity / mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / exocytosis / bioluminescence / generation of precursor metabolites and energy / sensory perception of sound / actin cytoskeleton / early endosome membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Aequorea victoria (jellyfish) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Miyata, Y. / Takahashi, K. / Lee, Y. / Sultan, C.S. / Kuribayashi, R. / Takahashi, M. / Hata, K. / Bamba, T. / Izumi, Y. / Liu, K. ...Miyata, Y. / Takahashi, K. / Lee, Y. / Sultan, C.S. / Kuribayashi, R. / Takahashi, M. / Hata, K. / Bamba, T. / Izumi, Y. / Liu, K. / Uemura, T. / Nomura, N. / Iwata, S. / Nagata, S. / Nishizawa, T. / Segawa, K. | ||||||
Funding support | Japan, 1items
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Citation | Journal: To Be Published Title: Mechanosensitive channel TMEM63B functions as a plasma membrane lipid scramblase Authors: Miyata, Y. / Takahashi, K. / Lee, Y. / Sultan, C.S. / Kuribayashi, R. / Takahashi, M. / Hata, K. / Bamba, T. / Izumi, Y. / Liu, K. / Uemura, T. / Nomura, N. / Iwata, S. / Nagata, S. / Nishizawa, T. / Segawa, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8wg3.cif.gz | 143.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8wg3.ent.gz | 100.8 KB | Display | PDB format |
PDBx/mmJSON format | 8wg3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8wg3_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 8wg3_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 8wg3_validation.xml.gz | 27.8 KB | Display | |
Data in CIF | 8wg3_validation.cif.gz | 39.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wg/8wg3 ftp://data.pdbj.org/pub/pdb/validation_reports/wg/8wg3 | HTTPS FTP |
-Related structure data
Related structure data | 37501MC 8wg4C 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: 126759.461 Da / Num. of mol.: 1 / Mutation: F64L,S65T,A206K,H231L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse), (gene. exp.) Aequorea victoria (jellyfish) Gene: Tmem63b, GFP / Cell line (production host): FreeStyle 293-F / Production host: Homo sapiens (human) / References: UniProt: Q3TWI9, UniProt: P42212 | ||||
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#2: Chemical | #3: Chemical | ChemComp-LBN / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: 2D ARRAY / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: mouse TMEM63B / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT | ||||||||||||
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Molecular weight | Value: 0.1 MDa / Experimental value: NO | ||||||||||||
Source (natural) |
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Source (recombinant) | Organism: Homo sapiens (human) / Cell: FreeStyle 293-F | ||||||||||||
Buffer solution | pH: 8 | ||||||||||||
Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1 | ||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 279 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: 1600 nm / Nominal defocus min: 800 nm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 110878 / Algorithm: BACK PROJECTION / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Accession code: Q3TWI9 / Source name: AlphaFold / Type: in silico model | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | Resolution: 3.4→3.4 Å / Cor.coef. Fo:Fc: 0.811 / SU B: 19.951 / SU ML: 0.324 / ESU R: 0.276 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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Solvent computation | Solvent model: PARAMETERS FOR MASK CACLULATION | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 148.666 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Total: 4586 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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