+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-3928 | |||||||||
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Title | Human mTORC2 core complex accessory factors | |||||||||
Map data | mTORC2 core complex accessory factor density | |||||||||
Sample |
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Function / homology | Function and homology information : / TORC2 signaling / : / regulation of peptidyl-serine phosphorylation / TORC2 complex / regulation of cellular response to oxidative stress / phosphatidic acid binding / negative regulation of Ras protein signal transduction / phosphatidylinositol-3,4-bisphosphate binding / phosphatidylinositol-3,5-bisphosphate binding ...: / TORC2 signaling / : / regulation of peptidyl-serine phosphorylation / TORC2 complex / regulation of cellular response to oxidative stress / phosphatidic acid binding / negative regulation of Ras protein signal transduction / phosphatidylinositol-3,4-bisphosphate binding / phosphatidylinositol-3,5-bisphosphate binding / regulation of establishment of cell polarity / embryo development ending in birth or egg hatching / positive regulation of actin filament polymerization / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / Constitutive Signaling by AKT1 E17K in Cancer / phosphatidylinositol-3,4,5-trisphosphate binding / cellular response to nutrient levels / CD28 dependent PI3K/Akt signaling / positive regulation of TOR signaling / cytoskeleton organization / phosphatidylinositol-4,5-bisphosphate binding / substantia nigra development / positive regulation of endothelial cell proliferation / protein serine/threonine kinase activator activity / VEGFR2 mediated vascular permeability / regulation of actin cytoskeleton organization / small GTPase binding / positive regulation of peptidyl-tyrosine phosphorylation / Regulation of TP53 Degradation / ribosome binding / PIP3 activates AKT signaling / positive regulation of peptidyl-serine phosphorylation / regulation of inflammatory response / cytoplasmic vesicle / actin cytoskeleton organization / positive regulation of cell growth / regulation of gene expression / peptidyl-serine phosphorylation / molecular adaptor activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell cycle / positive regulation of protein phosphorylation / phosphorylation / protein phosphorylation / negative regulation of apoptotic process / protein kinase binding / Golgi apparatus / nucleoplasm / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.2 Å | |||||||||
Authors | Scaiola A / Aylett CHS / Boehringer D / Stuttfeld E / Imseng S / Sauer E / Hall MN / Maier T / Ban N | |||||||||
Citation | Journal: Elife / Year: 2018 Title: Architecture of the human mTORC2 core complex. Authors: Edward Stuttfeld / Christopher Hs Aylett / Stefan Imseng / Daniel Boehringer / Alain Scaiola / Evelyn Sauer / Michael N Hall / Timm Maier / Nenad Ban / Abstract: The mammalian target of rapamycin (mTOR) is a key protein kinase controlling cellular metabolism and growth. It is part of the two structurally and functionally distinct multiprotein complexes mTORC1 ...The mammalian target of rapamycin (mTOR) is a key protein kinase controlling cellular metabolism and growth. It is part of the two structurally and functionally distinct multiprotein complexes mTORC1 and mTORC2. Dysregulation of mTOR occurs in diabetes, cancer and neurological disease. We report the architecture of human mTORC2 at intermediate resolution, revealing a conserved binding site for accessory proteins on mTOR and explaining the structural basis for the rapamycin insensitivity of the complex. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_3928.map.gz | 194 MB | EMDB map data format | |
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Header (meta data) | emd-3928-v30.xml emd-3928.xml | 12.8 KB 12.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_3928_fsc.xml | 13.7 KB | Display | FSC data file |
Images | emd_3928.png | 209.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-3928 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-3928 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_3928.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | mTORC2 core complex accessory factor density | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Human mTORC2 core complex accessory factors
Entire | Name: Human mTORC2 core complex accessory factors |
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Components |
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-Supramolecule #1: Human mTORC2 core complex accessory factors
Supramolecule | Name: Human mTORC2 core complex accessory factors / type: complex / ID: 1 / Parent: 0 Details: Accessory factor density for the mTORC2 core complex; Rictor, mSIN1 and Protor-1 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) / Recombinant cell: Sf9 / Recombinant plasmid: Multibac |
Molecular weight | Theoretical: 250 KDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 / Details: 150 mM NaCl, 15 mM NaBicine pH 8.0, 1 mM TCEP |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 |
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: Two seconds blotting. |
Details | Sample was prepared by a modified GRAFIX protocol described in the paper, and was extremely dilute. Particles were adhered to a thin carbon film to obtain reasonable coverage. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated magnification: 47100 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Specialist optics | Energy filter - Name: GIF Quantum SE |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Temperature | Min: 100.0 K / Max: 100.0 K |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Digitization - Sampling interval: 5.0 µm / Digitization - Frames/image: 1-40 / Number grids imaged: 1 / Number real images: 3997 / Average exposure time: 20.0 sec. / Average electron dose: 80.0 e/Å2 / Details: Dose weighting applied |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |