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Yorodumi- PDB-8srm: Structure of human ULK1 complex core (2:2:2 stoichiometry) of the... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8srm | |||||||||
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Title | Structure of human ULK1 complex core (2:2:2 stoichiometry) of the ATG13(450-517) mutant | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / Autophagy / Protein kinase / Complex | |||||||||
Function / homology | Function and homology information omegasome membrane / regulation of protein lipidation / glycophagy / neuron projection regeneration / negative regulation of collateral sprouting / Atg1/ULK1 kinase complex / response to mitochondrial depolarisation / positive regulation of autophagosome assembly / nucleophagy / protein localization to phagophore assembly site ...omegasome membrane / regulation of protein lipidation / glycophagy / neuron projection regeneration / negative regulation of collateral sprouting / Atg1/ULK1 kinase complex / response to mitochondrial depolarisation / positive regulation of autophagosome assembly / nucleophagy / protein localization to phagophore assembly site / piecemeal microautophagy of the nucleus / phagophore assembly site membrane / RAB GEFs exchange GTP for GDP on RABs / regulation of tumor necrosis factor-mediated signaling pathway / axon extension / phagophore assembly site / reticulophagy / TBC/RABGAPs / positive regulation of protein targeting to mitochondrion / Macroautophagy / Receptor Mediated Mitophagy / response to starvation / autophagosome membrane / cellular response to nutrient levels / mitophagy / autophagosome assembly / positive regulation of cell size / autophagosome / regulation of macroautophagy / negative regulation of protein-containing complex assembly / positive regulation of autophagy / protein-membrane adaptor activity / extrinsic apoptotic signaling pathway / protein serine/threonine kinase activator activity / liver development / negative regulation of extrinsic apoptotic signaling pathway / macroautophagy / Regulation of TNFR1 signaling / positive regulation of JNK cascade / peptidyl-threonine phosphorylation / protein localization / recycling endosome / small GTPase binding / autophagy / neuron projection development / GTPase binding / heart development / peptidyl-serine phosphorylation / nuclear membrane / mitochondrial outer membrane / protein autophosphorylation / lysosome / molecular adaptor activity / non-specific serine/threonine protein kinase / positive regulation of protein phosphorylation / cell cycle / axon / negative regulation of cell population proliferation / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / protein-containing complex binding / endoplasmic reticulum membrane / protein kinase binding / signal transduction / mitochondrion / ATP binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.46 Å | |||||||||
Authors | Chen, M. / Hurley, J.H. | |||||||||
Funding support | United States, 2items
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Citation | Journal: bioRxiv Title: Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex Authors: Chen, M. / Ren, X. / Cook, A. / Hurley, J.H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8srm.cif.gz | 179.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8srm.ent.gz | 119.5 KB | Display | PDB format |
PDBx/mmJSON format | 8srm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sr/8srm ftp://data.pdbj.org/pub/pdb/validation_reports/sr/8srm | HTTPS FTP |
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-Related structure data
Related structure data | 40735MC 8soiC 8sorC 8sqzC 8srqC 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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-Components
#1: Protein | Mass: 73325.633 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RB1CC1, KIAA0203, RBICC / Production host: Homo sapiens (human) / References: UniProt: Q8TDY2 #2: Protein | Mass: 24190.145 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ULK1, KIAA0722 / Production host: Homo sapiens (human) References: UniProt: O75385, non-specific serine/threonine protein kinase #3: Protein | Mass: 8150.997 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ATG13, KIAA0652 / Production host: Homo sapiens (human) / References: UniProt: O75143 |
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-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 autophagy initiation ULK1 complex core / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||||||||||||
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Molecular weight | Value: 0.21 MDa / Experimental value: YES | |||||||||||||||||||||||||
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.: 0.35 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Specimen support | Details: 25 mA / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-Electron microscopy imaging
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
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Microscopy | Model: FEI TALOS ARCTICA |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 36000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 2286 |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 968884 | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 148675 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||||||||||||||
Atomic model building | Source name: AlphaFold / Type: in silico model | ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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