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Open data
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Basic information
| Entry | Database: PDB / ID: 9h4q | ||||||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the SEAC wing - EGOC | ||||||||||||||||||||||||||||||||||||
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Keywords | SIGNALING PROTEIN / GTPase activating protein / GTPase / nutrient-sensing / amino acid signaling / cell growth | ||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationMTOR signalling / GATOR1 complex / pseudohyphal growth / Gtr1-Gtr2 GTPase complex / urea transport / negative regulation of small GTPase mediated signal transduction / Ragulator complex / microautophagy / protein localization to vacuolar membrane / protein localization to vacuole ...MTOR signalling / GATOR1 complex / pseudohyphal growth / Gtr1-Gtr2 GTPase complex / urea transport / negative regulation of small GTPase mediated signal transduction / Ragulator complex / microautophagy / protein localization to vacuolar membrane / protein localization to vacuole / Seh1-associated complex / Amino acids regulate mTORC1 / proline transport / regulation of TORC1 signaling / phosphate ion transport / regulation of autophagosome assembly / TORC1 signaling / endocytic recycling / vacuolar acidification / fungal-type vacuole membrane / negative regulation of TOR signaling / cellular response to nitrogen starvation / vacuolar membrane / transcription by RNA polymerase III / regulation of receptor recycling / positive regulation of TOR signaling / subtelomeric heterochromatin formation / transcription by RNA polymerase I / negative regulation of TORC1 signaling / signaling adaptor activity / positive regulation of TORC1 signaling / positive regulation of autophagy / negative regulation of autophagy / GTPase activator activity / cellular response to amino acid starvation / cellular response to starvation / meiotic cell cycle / cellular response to amino acid stimulus / late endosome membrane / late endosome / protein transport / cellular response to oxidative stress / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / chromosome, telomeric region / positive regulation of MAPK cascade / intracellular signal transduction / membrane raft / response to xenobiotic stimulus / GTPase activity / chromatin / GTP binding / signal transduction / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||||||||||||||||||||||||||
Authors | Tafur, L. / Loewith, R. | ||||||||||||||||||||||||||||||||||||
| Funding support | European Union, 1items
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Citation | Journal: To Be PublishedTitle: Structure and function of the yeast amino acid-sensing SEAC-EGOC supercomplex Authors: Tafur, L. / Bonadei, L. / Zheng, Y. / Loewith, R. | ||||||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9h4q.cif.gz | 738 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9h4q.ent.gz | 565.2 KB | Display | PDB format |
| PDBx/mmJSON format | 9h4q.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9h4q_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 9h4q_full_validation.pdf.gz | 1.7 MB | Display | |
| Data in XML | 9h4q_validation.xml.gz | 93.9 KB | Display | |
| Data in CIF | 9h4q_validation.cif.gz | 147.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h4/9h4q ftp://data.pdbj.org/pub/pdb/validation_reports/h4/9h4q | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 51867MC ![]() 9h5kC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 5 types, 5 molecules CXRUY
| #1: Protein | Mass: 131104.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #6: Protein | Mass: 182203.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 20266.086 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MEH1, EGO1, GSE2, YKR007W, YK106 / Production host: ![]() |
| #8: Protein | Mass: 8104.935 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: EGO2, YCR075W-A / Production host: ![]() |
| #9: Protein | Mass: 18371.877 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SLM4, EGO3, GSE1, YBR077C, YBR0723 / Production host: ![]() |
-GTP-binding protein ... , 2 types, 2 molecules ac
| #2: Protein | Mass: 35892.465 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: GTR1, YML121W, YM7056.05 / Production host: ![]() References: UniProt: Q00582, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
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| #3: Protein | Mass: 38633.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: GTR2, YGR163W / Production host: ![]() References: UniProt: P53290, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
-Nitrogen permease regulator ... , 2 types, 2 molecules Th
| #4: Protein | Mass: 69937.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #5: Protein | Mass: 130141.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 3 types, 4 molecules 




| #10: Chemical | ChemComp-MG / |
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| #11: Chemical | ChemComp-AF3 / |
| #12: Chemical |
-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Molecular weight |
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| Source (natural) |
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| Source (recombinant) | Organism: ![]() | ||||||||||||||||||||||||
| Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 133077 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
| Atomic model building |
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| Refine LS restraints |
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About Yorodumi






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FIELD EMISSION GUN

