+Open data
-Basic information
Entry | Database: PDB / ID: 7f4u | ||||||
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Title | Cryo-EM structure of TELO2-TTI1-TTI2 complex | ||||||
Components |
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Keywords | CHAPERONE / adaptor / TELO2 / TTI1 / TTI2 | ||||||
Function / homology | Function and homology information positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / 'de novo' cotranslational protein folding / TORC2 complex / TORC1 complex / regulation of TOR signaling / telomeric DNA binding / Hsp90 protein binding / chromosome, telomeric region / molecular adaptor activity ...positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / 'de novo' cotranslational protein folding / TORC2 complex / TORC1 complex / regulation of TOR signaling / telomeric DNA binding / Hsp90 protein binding / chromosome, telomeric region / molecular adaptor activity / nuclear body / protein stabilization / protein-containing complex binding / protein kinase binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.2 Å | ||||||
Authors | Cho, Y. / Kim, Y. | ||||||
Funding support | Korea, Republic Of, 1items
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Citation | Journal: J Mol Biol / Year: 2022 Title: Structure of the Human TELO2-TTI1-TTI2 Complex. Authors: Youngran Kim / Junhyeon Park / So Young Joo / Byung-Gyu Kim / Aera Jo / Hyunsook Lee / Yunje Cho / Abstract: Phosphatidylinositol 3-kinase-related protein kinases (PIKKs) play critical roles in various metabolic pathways related to cell proliferation and survival. The TELO2-TTI1-TTI2 (TTT) complex has been ...Phosphatidylinositol 3-kinase-related protein kinases (PIKKs) play critical roles in various metabolic pathways related to cell proliferation and survival. The TELO2-TTI1-TTI2 (TTT) complex has been proposed to recognize newly synthesized PIKKs and to deliver them to the R2TP complex (RUVBL1-RUVBL2-RPAP3-PIH1D1) and the heat shock protein 90 chaperone, thereby supporting their folding and assembly. Here, we determined the cryo-EM structure of the TTT complex at an average resolution of 4.2 Å. We describe the full-length structures of TTI1 and TELO2, and a partial structure of TTI2. All three proteins form elongated helical repeat structures. TTI1 provides a platform on which TELO2 and TTI2 bind to its central region and C-terminal end, respectively. The TELO2 C-terminal domain (CTD) is required for the interaction with TTI1 and recruitment of Ataxia-telangiectasia mutated (ATM). The N- and C-terminal segments of TTI1 recognize the FRAP-ATM-TRRAP (FAT) domain and the N-terminal HEAT repeats of ATM, respectively. The TELO2 CTD and TTI1 N- and C-terminal segments are required for cell survival in response to ionizing radiation. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7f4u.cif.gz | 219.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7f4u.ent.gz | 150 KB | Display | PDB format |
PDBx/mmJSON format | 7f4u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7f4u_validation.pdf.gz | 702.9 KB | Display | wwPDB validaton report |
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Full document | 7f4u_full_validation.pdf.gz | 724 KB | Display | |
Data in XML | 7f4u_validation.xml.gz | 35.8 KB | Display | |
Data in CIF | 7f4u_validation.cif.gz | 55.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f4/7f4u ftp://data.pdbj.org/pub/pdb/validation_reports/f4/7f4u | HTTPS FTP |
-Related structure data
Related structure data | 31454MC 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: 91846.883 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TELO2, KIAA0683 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9Y4R8 |
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#2: Protein | Mass: 117124.562 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TTI1, KIAA0406, SMG10 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O43156 |
#3: Protein | Mass: 54944.137 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TTI2, C8orf41 / Production host: Spodoptera frugiperda (fall armyworm) |
-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: chaperone adaptor / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Spodoptera frugiperda (fall armyworm) |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: DIFFRACTION / Nominal defocus max: 3500 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 42 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.15.2_3472: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 323679 / Symmetry type: POINT | ||||||||||||||||||||||||
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