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- EMDB-12979: Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-12979
TitleCryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex
Map dataStructure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone
Sample
  • Complex: TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex
    • Protein or peptide: RuvB-like 1
    • Protein or peptide: RuvB-like 2
    • Protein or peptide: TELO2-interacting protein 1 homolog,TELO2-interacting protein 1 homolog,TTI1
    • Protein or peptide: TELO2-interacting protein 2,TELO2-interacting protein 2,TTI2
    • Protein or peptide: Telomere length regulation protein TEL2 homolog
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
Function / homology
Function and homology information


: / positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / promoter-enhancer loop anchoring activity / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / establishment of protein localization to chromatin / R2TP complex / TORC2 complex / TORC1 complex ...: / positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / promoter-enhancer loop anchoring activity / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / establishment of protein localization to chromatin / R2TP complex / TORC2 complex / TORC1 complex / dynein axonemal particle / Swr1 complex / RPAP3/R2TP/prefoldin-like complex / regulation of TOR signaling / regulation of double-strand break repair / positive regulation of telomerase RNA localization to Cajal body / Ino80 complex / protein folding chaperone complex / box C/D snoRNP assembly / regulation of chromosome organization / telomeric DNA binding / NuA4 histone acetyltransferase complex / regulation of DNA replication / TFIID-class transcription factor complex binding / regulation of embryonic development / MLL1 complex / Telomere Extension By Telomerase / positive regulation of double-strand break repair via homologous recombination / telomere maintenance via telomerase / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA repair / Deposition of new CENPA-containing nucleosomes at the centromere / DNA helicase activity / positive regulation of DNA repair / TBP-class protein binding / telomere maintenance / cellular response to estradiol stimulus / Formation of the beta-catenin:TCF transactivating complex / DNA Damage Recognition in GG-NER / Hsp90 protein binding / euchromatin / negative regulation of canonical Wnt signaling pathway / chromatin DNA binding / ADP binding / beta-catenin binding / nuclear matrix / transcription corepressor activity / UCH proteinases / cellular response to UV / nucleosome / unfolded protein binding / positive regulation of canonical Wnt signaling pathway / protein folding / HATs acetylate histones / ATPase binding / spermatogenesis / regulation of apoptotic process / DNA recombination / DNA helicase / chromosome, telomeric region / molecular adaptor activity / transcription coactivator activity / nuclear body / protein stabilization / Ub-specific processing proteases / regulation of cell cycle / chromatin remodeling / ribonucleoprotein complex / cadherin binding / cell cycle / RNA polymerase II cis-regulatory region sequence-specific DNA binding / cell division / DNA repair / centrosome / protein-containing complex binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / protein kinase binding / positive regulation of DNA-templated transcription / protein homodimerization activity / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / extracellular exosome / nucleoplasm / ATP binding / membrane / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Tti2 family / Tti2 family / TEL2-interacting protein 1 / : / TELO2-interacting protein 1 / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily / Telomere length regulation protein / RuvB-like / RuvB-like, AAA-lid domain ...Tti2 family / Tti2 family / TEL2-interacting protein 1 / : / TELO2-interacting protein 1 / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily / Telomere length regulation protein / RuvB-like / RuvB-like, AAA-lid domain / RuvBL1/2, DNA/RNA binding domain / TIP49 P-loop domain / TIP49 AAA-lid domain / TIP49, P-loop domain / Armadillo-like helical / Armadillo-type fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
TELO2-interacting protein 1 homolog / TELO2-interacting protein 2 / RuvB-like 2 / RuvB-like 1 / Telomere length regulation protein TEL2 homolog
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.41 Å
AuthorsPal M / Llorca O / Pearl L
Funding support United Kingdom, Spain, 5 items
OrganizationGrant numberCountry
Wellcome Trust095605/Z/11/Z United Kingdom
Wellcome Trust095605/Z/11/A United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)BB/R01678X/1 United Kingdom
Spanish Ministry of Science, Innovation, and UniversitiesSAF2017-82632-P Spain
European Regional Development FundY2018/BIO4747 Spain
CitationJournal: Cell Rep / Year: 2021
Title: Structure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone.
Authors: Mohinder Pal / Hugo Muñoz-Hernandez / Dennis Bjorklund / Lihong Zhou / Gianluca Degliesposti / J Mark Skehel / Emma L Hesketh / Rebecca F Thompson / Laurence H Pearl / Oscar Llorca / Chrisostomos Prodromou /
Abstract: The R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1) complex, in collaboration with heat shock protein 90 (HSP90), functions as a chaperone for the assembly and stability of protein complexes, including RNA ...The R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1) complex, in collaboration with heat shock protein 90 (HSP90), functions as a chaperone for the assembly and stability of protein complexes, including RNA polymerases, small nuclear ribonucleoprotein particles (snRNPs), and phosphatidylinositol 3-kinase (PI3K)-like kinases (PIKKs) such as TOR and SMG1. PIKK stabilization depends on an additional complex of TELO2, TTI1, and TTI2 (TTT), whose structure and function are poorly understood. The cryoelectron microscopy (cryo-EM) structure of the human R2TP-TTT complex, together with biochemical experiments, reveals the mechanism of TOR recruitment to the R2TP-TTT chaperone. The HEAT-repeat TTT complex binds the kinase domain of TOR, without blocking its activity, and delivers TOR to the R2TP chaperone. In addition, TTT regulates the R2TP chaperone by inhibiting RUVBL1-RUVBL2 ATPase activity and by modulating the conformation and interactions of the PIH1D1 and RPAP3 components of R2TP. Taken together, our results show how TTT couples the recruitment of TOR to R2TP with the regulation of this chaperone system.
History
DepositionMay 19, 2021-
Header (metadata) releaseJul 7, 2021-
Map releaseJul 7, 2021-
UpdateOct 6, 2021-
Current statusOct 6, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0106
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0106
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7ole
  • Surface level: 0.0106
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7ole
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_12979.png

Downloads & links

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Map

FileDownload / File: emd_12979.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStructure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 280 pix.
= 299.6 Å		1.07 Å/pix.
x 280 pix.
= 299.6 Å		1.07 Å/pix.
x 280 pix.
= 299.6 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density

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Histogram (log scale)
Contour LevelBy AUTHOR: 0.0106 / Movie #1: 0.0106
Minimum - Maximum-0.018770417 - 0.053764913
Average (Standard dev.)0.00062394125 (±0.0026227725)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 299.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.071.071.07
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z299.600299.600299.600
α/β/γ90.00090.00090.000
start NX/NY/NZ192139186
NX/NY/NZ211274246
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.0190.0540.001

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Supplemental data

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Additional map: Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset1)...

Fileemd_12979_additional_1.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset1)
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Additional map: Cryo-EM structure of the TELO2-TTI1-TTI2 complex

Fileemd_12979_additional_2.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2 complex
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Additional map: Cryo-EM structure of the TELO2-TTI1-TTI2 complex

Fileemd_12979_additional_3.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2 complex
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Additional map: Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset1 halfmap1)...

Fileemd_12979_additional_4.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset1 halfmap1)
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Additional map: Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset1 halfmap2)...

Fileemd_12979_additional_5.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset1 halfmap2)
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Additional map: Composite map of the R2-TTT structure

Fileemd_12979_additional_6.map
AnnotationComposite map of the R2-TTT structure
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Half map: Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset2)...

Fileemd_12979_half_map_1.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset2)
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Half map: Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset2)...

Fileemd_12979_half_map_2.map
AnnotationCryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex (dataset2)
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Sample components

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Entire : TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex

EntireName: TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex
Components
  • Complex: TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex
    • Protein or peptide: RuvB-like 1
    • Protein or peptide: RuvB-like 2
    • Protein or peptide: TELO2-interacting protein 1 homolog,TELO2-interacting protein 1 homolog,TTI1
    • Protein or peptide: TELO2-interacting protein 2,TELO2-interacting protein 2,TTI2
    • Protein or peptide: Telomere length regulation protein TEL2 homolog
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex

SupramoleculeName: TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Molecular weightExperimental: 580 KDa

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Macromolecule #1: RuvB-like 1

MacromoleculeName: RuvB-like 1 / type: protein_or_peptide / ID: 1 / Details: ADP / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.296914 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGS KVPFCPMVGS EVYSTEIKKT EVLMENFRRA IGLRIKETKE VYEGEVTELT PCETENPMGG YGKTISHVII G LKTAKGTK ...String:
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGS KVPFCPMVGS EVYSTEIKKT EVLMENFRRA IGLRIKETKE VYEGEVTELT PCETENPMGG YGKTISHVII G LKTAKGTK QLKLDPSIFE SLQKERVEAG DVIYIEANSG AVKRQGRCDT YATEFDLEAE EYVPLPKGDV HKKKEIIQDV TL HDLDVAN ARPQGGQDIL SMMGQLMKPK KTEITDKLRG EINKVVNKYI DQGIAELVPG VLFVDEVHML DIECFTYLHR ALE SSIAPI VIFASNRGNC VIRGTEDITS PHGIPLDLLD RVMIIRTMLY TPQEMKQIIK IRAQTEGINI SEEALNHLGE IGTK TTLRY SVQLLTPANL LAKINGKDSI EKEHVEEISE LFYDAKSSAK ILADQQDKYM K

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Macromolecule #2: RuvB-like 2

MacromoleculeName: RuvB-like 2 / type: protein_or_peptide / ID: 2 / Details: ADP / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.222465 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMG MAQALGPDTP FTAIAGSEIF SLEMSKTEAL TQAFRRSIGV RIKEETEIIE GEVVEIQIDR PATGTGSKVG K LTLKTTEM ...String:
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMG MAQALGPDTP FTAIAGSEIF SLEMSKTEAL TQAFRRSIGV RIKEETEIIE GEVVEIQIDR PATGTGSKVG K LTLKTTEM ETIYDLGTKM IESLTKDKVQ AGDVITIDKA TGKISKLGRS FTRARDYDAM GSQTKFVQCP DGELQKRKEV VH TVSLHEI DVINSRTQGF LALFSGDTGE IKSEVREQIN AKVAEWREEG KAEIIPGVLF IDEVHMLDIE SFSFLNRALE SDM APVLIM ATNRGITRIR GTSYQSPHGI PIDLLDRLLI VSTTPYSEKD TKQILRIRCE EEDVEMSEDA YTVLTRIGLE TSLR YAIQL ITAASLVCRK RKGTEVQVDD IKRVYSLFLD ESRSTQYMKE YQDAFLFNEL KGETMDTS

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Macromolecule #3: TELO2-interacting protein 1 homolog,TELO2-interacting protein 1 h...

MacromoleculeName: TELO2-interacting protein 1 homolog,TELO2-interacting protein 1 homolog,TTI1
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 176.844344 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MAVFDTPEEA FGVLRPVCVQ LTKTQTVENV EHLQTRLQAV SDSALQELQQ YILFPLRFTL KTPGPKRERL IQSVVECLTF VLSSTCVKE QELLQELFSE LSACLYSPSS QKPAAVSEEL KLAVIQGLST LMHSAYGDII LTFYEPSILP RLGFAVSLLL G LAEQEKSK ...String:
MAVFDTPEEA FGVLRPVCVQ LTKTQTVENV EHLQTRLQAV SDSALQELQQ YILFPLRFTL KTPGPKRERL IQSVVECLTF VLSSTCVKE QELLQELFSE LSACLYSPSS QKPAAVSEEL KLAVIQGLST LMHSAYGDII LTFYEPSILP RLGFAVSLLL G LAEQEKSK QIKIAALKCL QVLLLQCDCQ DHPRSLDELE QKQLGDLFAS FLPGISTALT RLITGDFKQG HSIVVSSLKI FY KTVSFIM ADEQLKRISK VQAKPAVEHR VAELMVYREA DWVKKTGDKL TILIKKIIEC VSVHPHWKVR LELVELVEDL LLK CSQSLV ECAGPLLKAL VGLVNDESPE IQAQCNKVLR HFADQKVVVG NKALADILSE SLHSLATSLP RLMNSQDDQG KFST LSLLL GYLKLLGPKI NFVLNSVAHL QRLSKALIQV LELDVADIKI VEERRWNSDD LNASPKTSAT QPWNRIQRRY FRFFT DERI FMLLRQVCQL LGYYGNLYLL VDHFMELYHQ SVVYRKQAAM ILNELVTGAA GLEVEDLHEK HIKTNPEELR EIVTSI LEE YTSQENWYLV TCLETEEMGE ELMMEHPGLQ AITSGEHTCQ VTSFLAFSKP SPTICSMNSN IWQICIQLEG IGQFAYA LG KDFCLLLMSA LYPVLEKAGD QTLLISQVAT STMMDVCRAC GYDSLQHLIN QNSDYLVNGI SLNLRHLALH PHTPKVLE V MLRNSDANLL PLVADVVQDV LATLDQFYDK RAASFVSVLH ALMAALAQWF PDTGNLGHLQ EQSLGEEGSH LNQRPAALE KSTTTAEDIE QFLLNYLKEK DVADGNVSDF DNEEEEQSVP PKVDENDTRP DVEPPLPLQI QIAMDVMERC IHLLSDKNLQ IRLKVLDVL DLCVVVLQSH KNQLLPLAHQ AWPSLVHRLT RDAPLAVLRA FKVLRTLGSK CGDFLRSRFC KDVLPKLAGS L VTQAPISA RAGPVYSHTL AFKLQLAVLQ GLGPLCERLD LGEGDLNKVA DACLIYLSVK QPVKLQEAAR SVFLHLMKVD PD STWFLLN ELYCPVQFTP PHPSLHPVQL HGASGQQNPY TTNVLQLLKE LQ(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)(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)G(UNK)G(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)G(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)(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) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)G (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)(UNK)(UNK)(UNK)(UNK) (UNK)G(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)(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)(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)G(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)(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)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #4: TELO2-interacting protein 2,TELO2-interacting protein 2,TTI2

MacromoleculeName: TELO2-interacting protein 2,TELO2-interacting protein 2,TTI2
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 95.633781 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MELDSALEAP SQEDSNLSEE LSHSAFGQAF SKILHCLARP EARRGNVKDA VLKDLGDLIE ATEFDRLFEG TGARLRGMPE TLGQVAKAL EKYAAPSKEE EGGGDGHSEA AEKAAQVGLL FLKLLGKVET AKNSLVGPAW QTGLHHLAGP VYIFAITHSL E QPWTTPRS ...String:
MELDSALEAP SQEDSNLSEE LSHSAFGQAF SKILHCLARP EARRGNVKDA VLKDLGDLIE ATEFDRLFEG TGARLRGMPE TLGQVAKAL EKYAAPSKEE EGGGDGHSEA AEKAAQVGLL FLKLLGKVET AKNSLVGPAW QTGLHHLAGP VYIFAITHSL E QPWTTPRS REVAREVLTS LLQVTECGSV AGFLHGENED EKGRLSVILG LLKPDLYKES WKNNPAIKHV FSWTLQQVTR PW LSQHLER VLPASLVISD DYQTENKILG VHCLHHIVLN VPAADLLQYN RAQVLYHAIS NHLYTPEHHL IQAVLLCLLD LFP ILEKTL HWKGDGARPT THCDEVLRLI LTHMEPEHRL LLRRTYARNL PAFVNRLGIL TVRHLKRLER VIIGYLEVYD GPEE EARLK ILETLKLLMQ HTWPRVSCRL VVLLKALLKL ICDVARDPNL TPESVKSALL QEATDCLILL DRCSQGRVKG LLAKI PQSC EDRKVVNYIR KVQQVSEGAP YNGT(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)(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)G(UNK)G(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)G(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)(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)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)G (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)(UNK)(UNK)(UNK)(UNK)(UNK)G (UNK)(UNK)G (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)(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)

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Macromolecule #5: Telomere length regulation protein TEL2 homolog

MacromoleculeName: Telomere length regulation protein TEL2 homolog / type: protein_or_peptide / ID: 5 / Details: LGEMEPPALPREKEEFASAHF / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 53.424195 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MEPAPSEVRL AVREAIHALS SSEDGGHIFC TLESLKRYLG EMEPPALPRE (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)KEEFASAHF SPVLRCLASR LSPAWLELLP HGRLE(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) ...String:
MEPAPSEVRL AVREAIHALS SSEDGGHIFC TLESLKRYLG EMEPPALPRE (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)KEEFASAHF SPVLRCLASR LSPAWLELLP HGRLE(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)ELWASF FLEGPADQAF LVLMETIEGA AGPSFRLMKM ARLLARFLRE GRLAVLMEAQ CRQQTQPGF ILLRETLLGK VV(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)ALPDHLGNR LQQENLAEFF PQNYFRLLGE EVVRVLQAVV DSLQGGLDSS VSFVSQ VLG KACVHGRQQE ILGVLVPRLA ALTQGSYLHQ RVCWRLVEQV PDRAMEAVLT GLVEAALGPE VLSRLLGNLV VKNKKAQ FV MTQKLLFLQS RLTTPMLQSL LGHLAMDSQR RPLLLQVLKE LLETWGSSSA IRHTPLPQQR HVSKAVLICL AQLGEPEL R DSRDELLASM MAGVKCRLDS SLPPVRRLGM IVAEVVSARI HPEGPPLKFQ YEEDELSLEL LALASPQPAG DGASEAGT

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Macromolecule #6: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 5 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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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

Concentration1 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMHEPES2-[4-(2-Hydroxyethyl)-1-piperazinyl]-ethanesulfonic acid
140.0 mMNaClSodium Chroride

Details: Solutions were made fresh for protein purification
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 90 % / Chamber temperature: 287.15 K / Instrument: LEICA PLUNGER / Details: 3sec.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMin: 90.0 K / Max: 100.0 K
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 1034 pixel / Digitization - Dimensions - Height: 1034 pixel / Digitization - Sampling interval: 5.0 µm / Digitization - Frames/image: 1-40 / Number grids imaged: 10 / Number real images: 6000 / Average exposure time: 9.0 sec. / Average electron dose: 60.17 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated defocus max: 3.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus min: 1.2 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1000
CTF correctionSoftware - Name: RELION (ver. 3.1) / Software - details: CTFFIND
Final reconstructionNumber classes used: 200 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 3.41 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Software - details: RELION / Number images used: 267149
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 3.1) / Software - details: RELION
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 3.1) / Software - details: RELION
Final 3D classificationNumber classes: 200 / Avg.num./class: 100 / Software - Name: RELION (ver. 3.1) / Software - details: RELION
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6fo1

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-7ole:
Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex

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