+Open data
-Basic information
Entry | Database: PDB / ID: 9c7u | ||||||||||||
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Title | Structure of the human truncated BOS complex in GDN | ||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / membrane protein biogenesis / membrane protein complex | ||||||||||||
Function / homology | Function and homology information multi-pass transmembrane protein insertion into ER membrane / multi-pass translocon complex / regulation of protein complex stability / regulation of protein-containing complex assembly / regulation of signal transduction / ribosome binding / carbohydrate binding / membrane => GO:0016020 / protein stabilization / endoplasmic reticulum membrane ...multi-pass transmembrane protein insertion into ER membrane / multi-pass translocon complex / regulation of protein complex stability / regulation of protein-containing complex assembly / regulation of signal transduction / ribosome binding / carbohydrate binding / membrane => GO:0016020 / protein stabilization / endoplasmic reticulum membrane / protein-containing complex / membrane / plasma membrane Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.65 Å | ||||||||||||
Authors | Nguyen, V.N. / Tomaleri, G.P. / Voorhees, R.M. | ||||||||||||
Funding support | United States, 3items
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Citation | Journal: To Be Published Title: Role of a holo-insertase complex in the biogenesis of biophysically diverse ER membrane proteins Authors: Page, K.R. / Nguyen, V.N. / Pleiner, T. / Tomaleri, G.P. / Wang, M.L. / Guna, A. / Hazu, M. / Wang, T. / Chou, T. / Voorhees, R.M. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 9c7u.cif.gz | 172.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb9c7u.ent.gz | 129.8 KB | Display | PDB format |
PDBx/mmJSON format | 9c7u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c7/9c7u ftp://data.pdbj.org/pub/pdb/validation_reports/c7/9c7u | HTTPS FTP |
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-Related structure data
Related structure data | 45294MC 9c7vC C: citing same article (ref.) M: map data used to model this data |
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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: 63047.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NCLN / Production host: Homo sapiens (human) / References: UniProt: Q969V3 |
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#2: Protein | Mass: 42388.957 Da / Num. of mol.: 1 Fragment: UNP residues 1-36,873-1222 (Ig domains 1-9 deleted) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NOMO2 / Production host: Homo sapiens (human) / References: UniProt: Q5JPE7 |
#3: Protein | Mass: 25279.848 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TMEM147 / Production host: Homo sapiens (human) / References: UniProt: Q9BVK8 |
#4: Sugar | ChemComp-NAG / |
Has ligand of interest | N |
-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: Human truncated BOS complex / Type: COMPLEX Details: Human BOS complex of truncated NOMO (delta Ig 1-9), TMEM147, and NCLN Entity ID: #1-#3 / Source: RECOMBINANT | |||||||||||||||||||||||||||||||||||
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Molecular weight | Experimental value: NO | |||||||||||||||||||||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||||||||||||
Source (recombinant) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||||||||||||
Buffer solution | pH: 7.5 | |||||||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Sample solubilized and purified in GDN. | |||||||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / 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: SPOT SCAN |
Electron lens | Mode: DARK FIELD / Nominal magnification: 105000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 15929 |
EM imaging optics | Energyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.65 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 115841 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||
Atomic model building |
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