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- EMDB-31454: Cryo-EM structure of TELO2-TTI1-TTI2 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-31454
TitleCryo-EM structure of TELO2-TTI1-TTI2 complex
Map data
Sample
  • Complex: chaperone adaptor
    • Protein or peptide: Telomere length regulation protein TEL2 homolog
    • Protein or peptide: TELO2-interacting protein 1 homolog
    • Protein or peptide: TELO2-interacting protein 2
Function / homology
Function and homology information


positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / : / TORC2 complex / TORC1 complex / regulation of TOR signaling / telomeric DNA binding / telomere maintenance via telomerase / Hsp90 protein binding / chromosome, telomeric region ...positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / : / TORC2 complex / TORC1 complex / regulation of TOR signaling / telomeric DNA binding / telomere maintenance via telomerase / Hsp90 protein binding / chromosome, telomeric region / molecular adaptor activity / protein stabilization / nuclear body / chromatin remodeling / protein-containing complex binding / protein kinase binding / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
TEL2-interacting protein 1 / 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)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsCho Y / Kim Y
Funding support Korea, Republic Of, 1 items
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, 2021-
Header (metadata) releaseJun 22, 2022-
Map releaseJun 22, 2022-
UpdateJun 22, 2022-
Current statusJun 22, 2022Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_31454.png

Downloads & links

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Map

FileDownload / File: emd_31454.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.07 Å
Density
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.0020371953 - 1.9501892
Average (Standard dev.)0.00092386396 (±0.021619314)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 374.50003 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : chaperone adaptor

EntireName: chaperone adaptor
Components
  • Complex: chaperone adaptor
    • Protein or peptide: Telomere length regulation protein TEL2 homolog
    • Protein or peptide: TELO2-interacting protein 1 homolog
    • Protein or peptide: TELO2-interacting protein 2

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Supramolecule #1: chaperone adaptor

SupramoleculeName: chaperone adaptor / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Macromolecule #1: Telomere length regulation protein TEL2 homolog

MacromoleculeName: Telomere length regulation protein TEL2 homolog / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 91.846883 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MEPAPSEVRL AVREAIHALS SSEDGGHIFC TLESLKRYLG EMEPPALPRE KEEFASAHFS PVLRCLASRL SPAWLELLPH GRLEELWAS FFLEGPADQA FLVLMETIEG AAGPSFRLMK MARLLARFLR EGRLAVLMEA QCRQQTQPGF ILLRETLLGK V VALPDHLG ...String:
MEPAPSEVRL AVREAIHALS SSEDGGHIFC TLESLKRYLG EMEPPALPRE KEEFASAHFS PVLRCLASRL SPAWLELLPH GRLEELWAS FFLEGPADQA FLVLMETIEG AAGPSFRLMK MARLLARFLR EGRLAVLMEA QCRQQTQPGF ILLRETLLGK V VALPDHLG NRLQQENLAE FFPQNYFRLL GEEVVRVLQA VVDSLQGGLD SSVSFVSQVL GKACVHGRQQ EILGVLVPRL AA LTQGSYL HQRVCWRLVE QVPDRAMEAV LTGLVEAALG PEVLSRLLGN LVVKNKKAQF VMTQKLLFLQ SRLTTPMLQS LLG HLAMDS QRRPLLLQVL KELLETWGSS SAIRHTPLPQ QRHVSKAVLI CLAQLGEPEL RDSRDELLAS MMAGVKCRLD SSLP PVRRL GMIVAEVVSA RIHPEGPPLK FQYEEDELSL ELLALASPQP AGDGASEAGT SLVPATAEPP AETPAEIVDG GVPQA QLAG SDSDLDSDDE FVPYDMSGDR ELKSSKAPAY VRDCVEALTT SEDIERWEAA LRALEGLVYR SPTATREVSV ELAKVL LHL EEKTCVVGFA GLRQRALVAV TVTDPAPVAD YLTSQFYALN YSLRQRMDIL DVLTLAAQEL SRPGCLGRTP QPGSPSP NT PCLPEAAVSQ PGSAVASDWR VVVEERIRSK TQRLSKGGPR QGPAGSPSRF NSVAGHFFFP LLQRFDRPLV TFDLLGED Q LVLGRLAHTL GALMCLAVNT TVAVAMGKAL LEFVWALRFH IDAYVRQGLL SAVSSVLLSL PAARLLEDLM DELLEARSW LADVAEKDPD EDCRTLALRA LLLLQRLKNR LLPPASP

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Macromolecule #2: TELO2-interacting protein 1 homolog

MacromoleculeName: TELO2-interacting protein 1 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 117.124562 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MHHHHHMAVF DTPEEAFGVL RPVCVQLTKT QTVENVEHLQ TRLQAVSDSA LQELQQYILF PLRFTLKTPG PKRERLIQSV VECLTFVLS STCVKEQELL QELFSELSAC LYSPSSQKPA AVSEELKLAV IQGLSTLMHS AYGDIILTFY EPSILPRLGF A VSLLLGLA ...String:
MHHHHHMAVF DTPEEAFGVL RPVCVQLTKT QTVENVEHLQ TRLQAVSDSA LQELQQYILF PLRFTLKTPG PKRERLIQSV VECLTFVLS STCVKEQELL QELFSELSAC LYSPSSQKPA AVSEELKLAV IQGLSTLMHS AYGDIILTFY EPSILPRLGF A VSLLLGLA EQE(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)DCQDHP R(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)GDFKQGH SIVVSSLKIF YKTVSFIMAD EQLKRISKVQ AKPAVEHR V AELMVYREAD WVKKTGDKLT ILIKKIIECV SVHPHWKVRL ELVELVEDLL LKCSQSLVEC AGPLLKALVG LVNDESPEI QAQCNKVLRH FADQKVVVGN KALADILSES LHSLATSLPR LMNSQDDQGK FSTLSLLLGY LKLLGPKINF VLNSVAHLQR LSKALIQVL ELDVADIKIV EERRWNSDDL NASPKTSATQ PWNRIQRRYF RFFTDERIFM LLRQVCQLLG YYGNLYLLVD H FMELYHQS VVYRKQAAMI LNELVTGAAG LEVEDLHEKH IKTNPEELRE IVTSILEEYT SQENWYLVTC LETEEMGEEL MM EHPGLQA ITSGEHTCQV TSFLAFSKPS PTICSMNSNI WQICIQLEGI GQFAYALGKD FCLLLMSALY PVLEKAGDQT LLI SQVATS TMMDVCRACG YDSLQHLINQ NSDYLVNGIS LNLRHLALHP HTPKVLEVML RNSDANLLPL VADVVQDVLA TLDQ FYDKR AASFVSVLHA LMAALAQWFP DTGNLGHLQE QSLGEEGSHL NQRPAALEKS TTTAEDIEQF LLNYLKEKDV ADGNV SDFD NEEEEQSVPP KVDENDTRPD VEPPL(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)R LTRD(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)LVTQAP ISARAGPVYS H(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) LNKVADACLI YLSVKQP(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)GQQNP YTT NVLQLLKELQ

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Macromolecule #3: TELO2-interacting protein 2

MacromoleculeName: TELO2-interacting protein 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.944137 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MELDSALEAP SQEDSNLSEE LSHSAFGQAF SKILHCLARP (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) D AVLKDLGDLI EATEF(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK) ...String:
MELDSALEAP SQEDSNLSEE LSHSAFGQAF SKILHCLARP (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) D AVLKDLGDLI EATEF(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)VAKA LEKYAA(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)QVG LLF (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)LVG PAWQTGL(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) TPRSREVARE (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)FLH GENEDEKGRL SVILGLLKPD LYKESWKNNP AIKHVFSWTL QQVTRPW LS QHLERVLPAS LVISDDYQTE NKILGVHCLH HIVLNVPAAD LLQYNRAQVL YHAISNHLYT PEHHLIQAVL LCLLDLFP I LEKTLHWKGD GARPTTHCDE VLRLILTHME PEHRLLLRRT YARNLPAFVN RLGILTVRHL KRLERVIIGY LEVYDGPEE EARLKILETL KLLMQHTWPR VSCRLVVLLK ALLKLICDVA RDPNLTPESV KSALLQEATD CLILLDRCSQ GRVKGLLAKI PQSCEDRKV VNYIRKVQQV SEGAPYNGT

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: DIFFRACTION / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.0 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 42.0 e/Å2
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: ANGULAR RECONSTITUTION
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 323679

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