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- PDB-7f4u: Cryo-EM structure of TELO2-TTI1-TTI2 complex -

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Basic information

Entry
Database: PDB / ID: 7f4u
TitleCryo-EM structure of TELO2-TTI1-TTI2 complex
Components
  • TELO2-interacting protein 1 homolog
  • TELO2-interacting protein 2
  • Telomere length regulation protein TEL2 homolog
KeywordsCHAPERONE / adaptor / TELO2 / TTI1 / TTI2
Function / homology
Function and homology information


positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / TTT Hsp90 cochaperone complex / TORC2 complex / TORC1 complex / regulation of TOR signaling / telomeric DNA binding / Hsp90 protein binding / molecular adaptor activity / chromosome, telomeric region ...positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / TTT Hsp90 cochaperone complex / TORC2 complex / TORC1 complex / regulation of TOR signaling / telomeric DNA binding / Hsp90 protein binding / molecular adaptor activity / chromosome, telomeric region / protein stabilization / nuclear body / protein kinase binding / protein-containing complex binding / nucleus / membrane / cytoplasm / cytosol
Similarity search - Function
TEL2-interacting protein 1 / : / : / TELO2-interacting protein 1 / TTI1 N-terminal TPR domain / TELO2-interacting protein 1 homologue second TPR domain / TTI1 C-terminal TPR domain / TELO2 ARM repeat domain / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily ...TEL2-interacting protein 1 / : / : / TELO2-interacting protein 1 / TTI1 N-terminal TPR domain / TELO2-interacting protein 1 homologue second TPR domain / TTI1 C-terminal TPR domain / TELO2 ARM repeat domain / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily / : / Telomere length regulation protein / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
TELO2-interacting protein 1 homolog / Telomere length regulation protein TEL2 homolog
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsCho, Y. / Kim, Y.
Funding support Korea, Republic Of, 1items
OrganizationGrant numberCountry
National Research Foundation (NRF, Korea) Korea, Republic Of
CitationJournal: 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
DepositionJun 21, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 22, 2022Provider: repository / Type: Initial release
Revision 1.0Jun 22, 2022Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jun 22, 2022Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jun 22, 2022Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.0Jun 22, 2022Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jun 22, 2022Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Jun 12, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Revision 1.2Jul 2, 2025Group: Data collection / Structure summary / Category: em_admin / em_software / pdbx_entry_details / Item: _em_admin.last_update / _em_software.name
Revision 1.1Jul 2, 2025Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Data processing / Experimental summary / Data content type: EM metadata / EM metadata / Category: em_admin / em_software / Data content type: EM metadata / EM metadata / Item: _em_admin.last_update / _em_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Telomere length regulation protein TEL2 homolog
B: TELO2-interacting protein 1 homolog
C: TELO2-interacting protein 2


Theoretical massNumber of molelcules
Total (without water)263,9163
Polymers263,9163
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Telomere length regulation protein TEL2 homolog / Protein clk-2 homolog / hCLK2


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
#2: Protein TELO2-interacting protein 1 homolog / Protein SMG10


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 TELO2-interacting protein 2


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)
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: chaperone adaptor / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company
MicroscopyModel: FEI TALOS ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DIFFRACTION / Nominal defocus max: 3500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 42 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.15.2_3472: / Classification: refinement
EM softwareName: PHENIX / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 323679 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0038163
ELECTRON MICROSCOPYf_angle_d0.69911155
ELECTRON MICROSCOPYf_dihedral_angle_d134949
ELECTRON MICROSCOPYf_chiral_restr0.0341416
ELECTRON MICROSCOPYf_plane_restr0.0051470

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