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- PDB-9wjs: Tti1-Telo2 complex -

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Basic information

Entry
Database: PDB / ID: 9wjs
TitleTti1-Telo2 complex
Components
  • Telomere length regulation protein TEL2 homolog
  • Tti1
KeywordsCHAPERONE / Tti1 / Telo2 / CRYO-EM / TTT
Function / homology
Function and homology information


protein-containing complex stabilizing activity / positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / telomeric repeat DNA binding / Hsp90 protein binding / kinase binding / molecular adaptor activity / nuclear body / chromosome, telomeric region / protein stabilization ...protein-containing complex stabilizing activity / positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / telomeric repeat DNA binding / Hsp90 protein binding / kinase binding / molecular adaptor activity / nuclear body / chromosome, telomeric region / protein stabilization / protein kinase binding / protein-containing complex binding / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
: / TELO2 ARM repeat domain / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily / : / Telomere length regulation protein / Armadillo-type fold
Similarity search - Domain/homology
Telomere length regulation protein TEL2 homolog
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.83 Å
AuthorsQin, Y. / Wang, P. / Xu, G.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: GNB1L Chaperone Activity Licenses SAGA-Mediated Immune Evasion in Tumors
Authors: Qin, Y. / Xu, G.
History
DepositionAug 31, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Sep 2, 2026Provider: repository / Type: Initial release
Revision 1.0Sep 2, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tti1
C: Telomere length regulation protein TEL2 homolog


Theoretical massNumber of molelcules
Total (without water)131,3712
Polymers131,3712
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Tti1


Mass: 82665.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: unidentified baculovirus
#2: Protein Telomere length regulation protein TEL2 homolog / Protein clk-2 homolog / hCLK2


Mass: 48705.742 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TELO2, KIAA0683 / Production host: unidentified baculovirus / References: UniProt: Q9Y4R8
Has protein modificationN

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Tti1-Telo2 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: unidentified baculovirus
Buffer solutionpH: 7.5
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: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM software
IDNameCategory
1Gautomatchparticle selection
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.83 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 287635 / Symmetry type: POINT

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