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- EMDB-14199: Refined, unsharpened map of human telomerase-DNA-TPP1-POT1 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-14199
TitleRefined, unsharpened map of human telomerase-DNA-TPP1-POT1 complex
Map dataRefined unsharpened map of telomerase-TPP1-Pot1-DNA
Sample
  • Complex: Complex of telomeric DNA-bound human telomerase with TPP1 and Pot1
    • Protein or peptide: Telomerase reverse transcriptase
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • Protein or peptide: TPP1
    • Protein or peptide: POT1
    • RNA: human telomerase RNA
    • DNA: Telomeric DNA
KeywordsReverse transcriptase / ribonucleoprotein / telomerase / telomere / DNA BINDING PROTEIN
Function / homology
Function and homology information


positive regulation of DNA strand elongation / regulation of DNA helicase activity / positive regulation of DNA helicase activity / G-rich single-stranded DNA binding / telomere assembly / positive regulation of hair cycle / template-free RNA nucleotidyltransferase / positive regulation of transdifferentiation / TERT-RMRP complex / DNA strand elongation ...positive regulation of DNA strand elongation / regulation of DNA helicase activity / positive regulation of DNA helicase activity / G-rich single-stranded DNA binding / telomere assembly / positive regulation of hair cycle / template-free RNA nucleotidyltransferase / positive regulation of transdifferentiation / TERT-RMRP complex / DNA strand elongation / RNA-directed RNA polymerase complex / siRNA transcription / positive regulation of protein localization to nucleolus / 8-hydroxy-2'-deoxyguanosine DNA binding / telomeric D-loop binding / regulation of double-strand break repair via nonhomologous end joining / positive regulation of helicase activity / telomerase catalytic core complex / RNA-templated DNA biosynthetic process / : / telomerase inhibitor activity / DEAD/H-box RNA helicase binding / establishment of protein localization to telomere / telomerase activity / telomeric D-loop disassembly / shelterin complex / Telomere C-strand synthesis initiation / regulation of telomere maintenance via telomerase / Telomere C-strand (Lagging Strand) Synthesis / : / positive regulation of telomere maintenance / nuclear telomere cap complex / single-stranded telomeric DNA binding / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / siRNA processing / G-rich strand telomeric DNA binding / telomere capping / telomerase holoenzyme complex / positive regulation of vascular associated smooth muscle cell migration / telomerase RNA binding / DNA duplex unwinding / DNA biosynthetic process / RNA-templated transcription / telomeric DNA binding / positive regulation of stem cell proliferation / mitochondrial nucleoid / negative regulation of cellular senescence / negative regulation of telomere maintenance via telomerase / Telomere Extension By Telomerase / telomere maintenance via telomerase / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / replicative senescence / positive regulation of Wnt signaling pathway / positive regulation of G1/S transition of mitotic cell cycle / negative regulation of endothelial cell apoptotic process / response to cadmium ion / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / : / positive regulation of vascular associated smooth muscle cell proliferation / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / positive regulation of telomere maintenance via telomerase / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere maintenance / mitochondrion organization / positive regulation of nitric-oxide synthase activity / positive regulation of glucose import / Formation of the beta-catenin:TCF transactivating complex / regulation of protein stability / DNA Damage/Telomere Stress Induced Senescence / PML body / transcription coactivator binding / positive regulation of miRNA transcription / RNA-directed DNA polymerase / structural constituent of chromatin / positive regulation of angiogenesis / RNA-directed DNA polymerase activity / nucleosome / positive regulation of protein binding / protein-folding chaperone binding / cellular response to hypoxia / negative regulation of neuron apoptotic process / chromosome, telomeric region / tRNA binding / nuclear body / nuclear speck / protein heterodimerization activity / negative regulation of gene expression / RNA-dependent RNA polymerase activity / nucleolus / protein homodimerization activity / DNA binding / RNA binding / nucleoplasm / identical protein binding
Similarity search - Function
: / Protection of telomeres protein 1 (POT1), C-terminal insertion domain / Shelterin complex subunit TPP1/Est3 / Shelterin complex subunit, TPP1/ACD / Adrenocortical dysplasia protein / : / Telomerase reverse transcriptase, C-terminal extension / Protection of telomeres protein 1, ssDNA-binding domain / ssDNA-binding domain of telomere protection protein / Protection of telomeres protein 1 ...: / Protection of telomeres protein 1 (POT1), C-terminal insertion domain / Shelterin complex subunit TPP1/Est3 / Shelterin complex subunit, TPP1/ACD / Adrenocortical dysplasia protein / : / Telomerase reverse transcriptase, C-terminal extension / Protection of telomeres protein 1, ssDNA-binding domain / ssDNA-binding domain of telomere protection protein / Protection of telomeres protein 1 / Telomerase ribonucleoprotein complex - RNA binding domain / Telomeric single stranded DNA binding POT1/Cdc13 / Telomeric single stranded DNA binding POT1/CDC13 / Telomeric single stranded DNA binding POT1/CDC13 / Telomerase reverse transcriptase / Telomerase ribonucleoprotein complex - RNA-binding domain / Telomerase ribonucleoprotein complex - RNA binding domain / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Histone-fold / Nucleic acid-binding, OB-fold / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
Adrenocortical dysplasia homolog (Mouse), isoform CRA_a / Histone H2A / Histone H2B / Telomerase reverse transcriptase / Protection of telomeres protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsSekne Z / Ghanim GE / van Roon AMM / Nguyen THD
Funding support United Kingdom, United States, 2 items
OrganizationGrant numberCountry
UK Research and Innovation (UKRI)MC_UP_1201/19 United Kingdom
Jane Coffin Childs Postdoctoral Fellowship United States
CitationJournal: Science / Year: 2022
Title: Structural basis of human telomerase recruitment by TPP1-POT1.
Authors: Zala Sekne / George E Ghanim / Anne-Marie M van Roon / Thi Hoang Duong Nguyen /
Abstract: Telomerase maintains genome stability by extending the 3' telomeric repeats at eukaryotic chromosome ends, thereby counterbalancing progressive loss caused by incomplete genome replication. In ...Telomerase maintains genome stability by extending the 3' telomeric repeats at eukaryotic chromosome ends, thereby counterbalancing progressive loss caused by incomplete genome replication. In mammals, telomerase recruitment to telomeres is mediated by TPP1, which assembles as a heterodimer with POT1. We report structures of DNA-bound telomerase in complex with TPP1 and with TPP1-POT1 at 3.2- and 3.9-angstrom resolution, respectively. Our structures define interactions between telomerase and TPP1-POT1 that are crucial for telomerase recruitment to telomeres. The presence of TPP1-POT1 stabilizes the DNA, revealing an unexpected path by which DNA exits the telomerase active site and a DNA anchor site on telomerase that is important for telomerase processivity. Our findings rationalize extensive prior genetic and biochemical findings and provide a framework for future mechanistic work on telomerase regulation.
History
DepositionJan 26, 2022-
Header (metadata) releaseMar 2, 2022-
Map releaseMar 2, 2022-
UpdateDec 13, 2023-
Current statusDec 13, 2023Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0065
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.0065
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_14199.png

Downloads & links

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Map

FileDownload / File: emd_14199.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRefined unsharpened map of telomerase-TPP1-Pot1-DNA
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 280 pix.
= 305.2 Å		1.09 Å/pix.
x 280 pix.
= 305.2 Å		1.09 Å/pix.
x 280 pix.
= 305.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0065 / Movie #1: 0.0065
Minimum - Maximum-0.014908087 - 0.046081334
Average (Standard dev.)0.00012686482 (±0.0018475773)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 305.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.091.091.09
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z305.200305.200305.200
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ640640640
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.0150.0460.000

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Supplemental data

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Sample components

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Entire : Complex of telomeric DNA-bound human telomerase with TPP1 and Pot1

EntireName: Complex of telomeric DNA-bound human telomerase with TPP1 and Pot1
Components
  • Complex: Complex of telomeric DNA-bound human telomerase with TPP1 and Pot1
    • Protein or peptide: Telomerase reverse transcriptase
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • Protein or peptide: TPP1
    • Protein or peptide: POT1
    • RNA: human telomerase RNA
    • DNA: Telomeric DNA

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Supramolecule #1: Complex of telomeric DNA-bound human telomerase with TPP1 and Pot1

SupramoleculeName: Complex of telomeric DNA-bound human telomerase with TPP1 and Pot1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Telomerase reverse transcriptase

MacromoleculeName: Telomerase reverse transcriptase / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDP AAFRA LVAQCLVCVP WDARPPPAAP SFRQVSCLKE LVARVLQRLC ERGAKNVLAF GFA LLDGAR GGPPEAFTTS VRSYLPNTVT DALRGSGAWG LLLRRVGDDV LVHLLARCAL FV LVAPSCA ...String:
MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDP AAFRA LVAQCLVCVP WDARPPPAAP SFRQVSCLKE LVARVLQRLC ERGAKNVLAF GFA LLDGAR GGPPEAFTTS VRSYLPNTVT DALRGSGAWG LLLRRVGDDV LVHLLARCAL FV LVAPSCA YQVCGPPLYQ LGAATQARPP PHASGPRRRL GCERAWNHSV REAGVPLGLP A PGARRRGG SASRSLPLPK RPRRGAAPEP ERTPVGQGSW AHPGRTRGPS DRGFCVVSPA RPAEEATSL EGALSGTRHS HPSVGRQHHA GPPSTSRPPR PWDTPCPPVY AETKHFLYS SGDKEQLRPS FLLSSLRPSL TGARRLVETI FLGSRPWMPG TPRRLPRLPQ RYWQMRPL F LELLGNHAQC PYGVLLKTHC PLRAAVTPAA GVCAREKPQG SVAAPEEEDT DPRRLVQ LL RQHSSPWQVY GFVRACLRRL VPPGLWGSRH NERRFLRNTK KFISLGKHAK LSLQEL TWK MSVRDCAWLR RSPGVGCVPA AEHRLREEIL AKFLHWLMSV YVVELLRSFF YVTET TFQK NRLFFYRKSV WSKLQSIGIR QHLKRVQLRE LSEAEVRQHR EARPALLTSR LRFI PKPDG LRPIVNMDYV VGARTFRREK RAERLTSRVK ALFSVLNYER ARRPGLLGAS VLG LDDIHR AWRTFVLRVR AQDPPPELYF VKVDVTGAYD TIPQDRLTEV IASIIKPQNT YC VRRYAVV QKAAHGHVRK AFKSHVSTLT DLQPYMRQFV AHLQETSPLR DAVVIEQSSS L NEASSGLF DVFLRFMCHH AVRIRGKSYV QCQGIPQGSI LSTLLCSLCY GDMENKLFAG IRRDGLLLR LVDDFLLVTP HLTHAKTFLR TLVRGVPEYG CVVNLRKTVV NFPVEDEAL GGTAFVQMPA HGLFPWCGLL LDTRTLEVQS DYSSYARTSI RASLTFNRGF KAGRNMRR K LFGVLRLKCH SLFLDLQVNS LQTVCTNIYK ILLLQAYRFH ACVLQLPFHQ QVWKNPT FF LRVISDTASL CYSILKAKNA GMSLGAKGAA GPLPSEAVQW LCHQAFLLKL TRHRVT YVP LLGSLRTAQT QLSRKLPGTT LTALEAAANP ALPSDFKTIL D

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Macromolecule #2: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney / Tissue: Kidney
SequenceString:
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VRRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG KVTIAQGGVL PNIQAVLLPK K TESHHKAK GK

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Macromolecule #3: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney / Tissue: Kidney
SequenceString:
MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVND IFERIAGEAS RLAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV T KYTSSNPR NLSPTKPGGS EDRQPPPSQL SAIPPFCLVL RAGIAGQV

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Macromolecule #4: TPP1

MacromoleculeName: TPP1 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera (butterflies/moths)
SequenceString: MAGSGRLVLR PWIRELILGS ETPSSPRAGQ LLEVLQDAEA AVAGPSHAPD TSDVGATLLV SDGTHSVRC LVTREALDTS DWEEKEFGFR GTEGRLLLLQ DCGVHVQVAE GGAPAEFYLQ V DRFSLLPT EQPRLRVPGC NQDLDVQKKL YDCLEEHLSE STSSNAGLSL ...String:
MAGSGRLVLR PWIRELILGS ETPSSPRAGQ LLEVLQDAEA AVAGPSHAPD TSDVGATLLV SDGTHSVRC LVTREALDTS DWEEKEFGFR GTEGRLLLLQ DCGVHVQVAE GGAPAEFYLQ V DRFSLLPT EQPRLRVPGC NQDLDVQKKL YDCLEEHLSE STSSNAGLSL SQLLDEMRED QE HQGALVC LAESCLTLEG PCTAPPVTHW AASRCKATGE AVYTVPSSML CISENDQLIL SSL GPCQRT QGPELPPPDP ALQDLSLTLI ASPPSSPSSS GTPALPGHMS SEESGTSISL LPAL SLAAP DPGQRSSSQP SPAICSAPAT LTPRSPHASR TPSSPLQSCT PSLSPRSHVP SPHQA LVTR PQKPSLEFKE FVGLPCKNRP PFPRTGATRG AQEPCSVWEP PKRHRDGSAF QYEYEP PCT SLCARVQAVR LPPQLMAWAL HFLMDAQPGS EPTPM

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Macromolecule #5: POT1

MacromoleculeName: POT1 / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera (butterflies/moths)
SequenceString: MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV DQTNVKLTCL LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG FASLTFEGTL GAPIIPRTSS KYFNFTTEDH KMVEALRVWA STHMSPSWTL LKLCDVQPMQ YFDLTCQLLG ...String:
MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV DQTNVKLTCL LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG FASLTFEGTL GAPIIPRTSS KYFNFTTEDH KMVEALRVWA STHMSPSWTL LKLCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RSLKVGSFLR IYSLHTKLQS MNSENQTMLS LEFHLHGGTS YGRGIRVLPE SNSDVDQLKK DLESANLTAN QHSDVICQSE PDDSFPSSGS VSLYEVERCQ QLSATILTDH QYLERTPLCA ILKQKAPQQY RIRAKLRSYK PRRLFQSVKL HCPKCHLLQE VPHEGDLDII FQDGATKTPD VKLQNTSLYD SKIWTTKNQK GRKVAVHFVK NNGILPLSNE CLLLIEGGTL SEICKLSNKF NSVIPVRSGH EDLELLDLSA PFLIQGTIHH YGCKQCSSLR SIQNLNSLVD KTSWIPSSVA EALGIVPLQY VFVMTFTLDD GTGVLEAYLM DSDKFFQIPA SEVLMDDDLQ KSVDMIMDMF CPPGIKIDAY PWLECFIKSY NVTNGTDNQI CYQIFDTTVA EDVI

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Macromolecule #6: human telomerase RNA

MacromoleculeName: human telomerase RNA / type: rna / ID: 6
Source (natural)Organism: Homo sapiens (human)
SequenceString: GGGUUGCGGA GGGUGGGCCU GGGAGGGGUG GUGGCCAUUU UUUGUCUAAC CCUAACUGAG AAGGGCGUAG GCGCCGUGC UUUUGCUCCC CGCGCGCUGU UUUUCUCGCU GACUUUCAGC GGGCGGAAAA GCCUCGGCCU G CCGCCUUC CACCGUUCAU UCUAGAGCAA ...String:
GGGUUGCGGA GGGUGGGCCU GGGAGGGGUG GUGGCCAUUU UUUGUCUAAC CCUAACUGAG AAGGGCGUAG GCGCCGUGC UUUUGCUCCC CGCGCGCUGU UUUUCUCGCU GACUUUCAGC GGGCGGAAAA GCCUCGGCCU G CCGCCUUC CACCGUUCAU UCUAGAGCAA ACAAAAAAUG UCAGCUGCUG GCCCGUUCGC CCCUCCCGGG GA CCUGCGG CGGGUCGCCU GCCCAGCCCC CGAACCCCGC CUGGAGGCCG CGGUCGGCCC GGGGCUUCUC CGG AGGCAC CCACUGCCAC CGCGAAGAGU UGGGCUCUGU CAGCCGCGGG UCUCUCGGGG GCGAGGGCGA GGUU CAGGC CUUUCAGGCC GCAGGAAGAG GAACGGAGCG AGUCCCCGCG CGCGGCGCGA UUCCCUGAGC UGUGG GACG UGCACCCAGG ACUCGGCUCA CACAUGC

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Macromolecule #7: Telomeric DNA

MacromoleculeName: Telomeric DNA / type: dna / ID: 7 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
SequenceString:
TTAGGGTTAG GGTTAGGGTT AGGGTTAGGG

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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
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
150.0 mMNaClsodium chloride
10.0 %C3H8O3glycerol
2.0 mMMgCl2magnesium chloride
0.05 %IGEPAL CA630
1.0 %C12H22O11trehalose
1.0 mMC4H10O2S2DTT
GridModel: C-flat / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 5 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 3 / Number real images: 50775 / Average exposure time: 3.0 sec. / Average electron dose: 48.0 e/Å2
Details: Images were collected in movie-mode and fractionated into 48 movie frames
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated magnification: 45872 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
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: 21589656
Startup modelType of model: EMDB MAP
EMDB ID:

12174

Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number images used: 192871
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4)
Final 3D classificationSoftware - Name: RELION (ver. 4)

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Atomic model buiding 1

Initial modelPDB ID:

7bg9


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: RECIPROCAL / Protocol: AB INITIO MODEL

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