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- PDB-9wjy: Tti2-Tti1-C -

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Basic information

Entry
Database: PDB / ID: 9wjy
TitleTti2-Tti1-C
Components
  • TELO2-interacting protein 1 homolog
  • TELO2-interacting protein 2
KeywordsCHAPERONE / Tti1 / Tti2 / TTT
Function / homology
Function and homology information


protein-containing complex stabilizing activity / positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / TORC2 complex / TORC1 complex / regulation of TOR signaling / kinase binding / protein stabilization / nucleus / cytoplasm
Similarity search - Function
Tti2 family / Tti2 family / TEL2-interacting protein 1 / : / : / : / : / TELO2-interacting protein 1 / TTI1 N-terminal TPR domain / TELO2-interacting protein 1 homologue second TPR domain ...Tti2 family / Tti2 family / 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 / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
TELO2-interacting protein 1 homolog / TELO2-interacting protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsQin, Y. / 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

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Assembly

Deposited unit
A: TELO2-interacting protein 1 homolog
B: TELO2-interacting protein 2


Theoretical massNumber of molelcules
Total (without water)102,5692
Polymers102,5692
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 TELO2-interacting protein 1 homolog / Protein SMG10


Mass: 47620.535 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: Baculovirus expression vector pFastBac1-HM / References: UniProt: O43156
#2: Protein TELO2-interacting protein 2


Mass: 54948.457 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TTI2, C8orf41 / Production host: unidentified baculovirus / References: UniProt: Q6NXR4
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-Tti2 complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
11Baculovirus expression vector pFastBac1-HM274590
21unidentified baculovirus10469
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: 300 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k)

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Processing

EM software
IDNameCategory
1Gautomatchparticle selection
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 107543 / Symmetry type: POINT

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