+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31454 | |||||||||
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Title | Cryo-EM structure of TELO2-TTI1-TTI2 complex | |||||||||
Map data | ||||||||||
Sample |
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Keywords | adaptor / CHAPERONE / 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 / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
Authors | Cho Y / Kim Y | |||||||||
Funding support | Korea, Republic Of, 1 items
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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
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_31454.map.gz | 145.4 MB | EMDB map data format | |
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Header (meta data) | emd-31454-v30.xml emd-31454.xml | 14.3 KB 14.3 KB | Display Display | EMDB header |
Images | emd_31454.png | 67 KB | ||
Filedesc metadata | emd-31454.cif.gz | 6.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31454 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31454 | HTTPS FTP |
-Validation report
Summary document | emd_31454_validation.pdf.gz | 337.1 KB | Display | EMDB validaton report |
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Full document | emd_31454_full_validation.pdf.gz | 336.7 KB | Display | |
Data in XML | emd_31454_validation.xml.gz | 6.8 KB | Display | |
Data in CIF | emd_31454_validation.cif.gz | 7.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31454 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31454 | HTTPS FTP |
-Related structure data
Related structure data | 7f4uMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_31454.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : chaperone adaptor
Entire | Name: chaperone adaptor |
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Components |
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-Supramolecule #1: chaperone adaptor
Supramolecule | Name: chaperone adaptor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Telomere length regulation protein TEL2 homolog
Macromolecule | Name: Telomere length regulation protein TEL2 homolog / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 91.846883 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: 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 UniProtKB: Telomere length regulation protein TEL2 homolog |
-Macromolecule #2: TELO2-interacting protein 1 homolog
Macromolecule | Name: TELO2-interacting protein 1 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 117.124562 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: 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 UniProtKB: TELO2-interacting protein 1 homolog |
-Macromolecule #3: TELO2-interacting protein 2
Macromolecule | Name: TELO2-interacting protein 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 54.944137 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | 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) ...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 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 42.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DIFFRACTION / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 323679 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: ANGULAR RECONSTITUTION |