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- EMDB-26863: Tetrahymena telomerase with CST -

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Basic information

Entry
Database: EMDB / ID: EMD-26863
TitleTetrahymena telomerase with CST
Map dataTetrahymena telomerase with CST
Sample
  • Complex: Tetrahymena telomerase holoenzyme
    • Protein or peptide: x 9 types
    • RNA: x 1 types
    • DNA: x 1 types
  • Ligand: x 1 types
Keywordstelomerase / RNP / CST / REPLICATION
Function / homology
Function and homology information


telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase RNA reverse transcriptase activity / DNA replication factor A complex / single-stranded telomeric DNA binding / telomerase RNA binding / telomerase holoenzyme complex / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase ...telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase RNA reverse transcriptase activity / DNA replication factor A complex / single-stranded telomeric DNA binding / telomerase RNA binding / telomerase holoenzyme complex / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / DNA recombination / DNA replication / chromosome, telomeric region / DNA repair / DNA binding / zinc ion binding / metal ion binding
Similarity search - Function
Telomerase reverse transcriptase TEN domain / Replication factor A protein 3 / Replication factor A protein 3 / xRRM domain profile. / La protein, xRRM domain / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function / La-type HTH domain / La-type HTH domain profile. ...Telomerase reverse transcriptase TEN domain / Replication factor A protein 3 / Replication factor A protein 3 / xRRM domain profile. / La protein, xRRM domain / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function / La-type HTH domain / La-type HTH domain profile. / Telomerase ribonucleoprotein complex - RNA binding domain / : / Telomerase reverse transcriptase / Telomerase ribonucleoprotein complex - RNA-binding domain / Telomerase ribonucleoprotein complex - RNA binding domain / Replication factor A, C-terminal / Replication factor-A C terminal domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Winged helix DNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
Replication protein A 32 kDa subunit / Replication protein A 14 kDa subunit / Telomerase-associated protein of 75 kDa / Telomeric repeat-binding subunit 1 / Telomerase-associated protein of 19 kDa / Telomerase-associated protein of 50 kDa / Telomerase reverse transcriptase / Telomerase-associated protein of 45 kDa / La-related protein 7 homolog
Similarity search - Component
Biological speciesTetrahymena thermophila (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsHe Y / Song H / Chan H / Wang Y / Liu B / Susac L / Zhou ZH / Feigon J
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM131901 United States
National Science Foundation (NSF, United States)MCB2016540 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM071940 United States
CitationJournal: Nature / Year: 2022
Title: Structure of Tetrahymena telomerase-bound CST with polymerase α-primase.
Authors: Yao He / He Song / Henry Chan / Baocheng Liu / Yaqiang Wang / Lukas Sušac / Z Hong Zhou / Juli Feigon /
Abstract: Telomeres are the physical ends of linear chromosomes. They are composed of short repeating sequences (such as TTGGGG in the G-strand for Tetrahymena thermophila) of double-stranded DNA with a single- ...Telomeres are the physical ends of linear chromosomes. They are composed of short repeating sequences (such as TTGGGG in the G-strand for Tetrahymena thermophila) of double-stranded DNA with a single-strand 3' overhang of the G-strand and, in humans, the six shelterin proteins: TPP1, POT1, TRF1, TRF2, RAP1 and TIN2. TPP1 and POT1 associate with the 3' overhang, with POT1 binding the G-strand and TPP1 (in complex with TIN2) recruiting telomerase via interaction with telomerase reverse transcriptase (TERT). The telomere DNA ends are replicated and maintained by telomerase, for the G-strand, and subsequently DNA polymerase α-primase (PolαPrim), for the C-strand. PolαPrim activity is stimulated by the heterotrimeric complex CTC1-STN1-TEN1 (CST), but the structural basis of the recruitment of PolαPrim and CST to telomere ends remains unknown. Here we report cryo-electron microscopy (cryo-EM) structures of Tetrahymena CST in the context of the telomerase holoenzyme, in both the absence and the presence of PolαPrim, and of PolαPrim alone. Tetrahymena Ctc1 binds telomerase subunit p50, a TPP1 orthologue, on a flexible Ctc1 binding motif revealed by cryo-EM and NMR spectroscopy. The PolαPrim polymerase subunit POLA1 binds Ctc1 and Stn1, and its interface with Ctc1 forms an entry port for G-strand DNA to the POLA1 active site. We thus provide a snapshot of four key components that are required for telomeric DNA synthesis in a single active complex-telomerase-core ribonucleoprotein, p50, CST and PolαPrim-that provides insights into the recruitment of CST and PolαPrim and the handoff between G-strand and C-strand synthesis.
History
DepositionMay 6, 2022-
Header (metadata) releaseJul 13, 2022-
Map releaseJul 13, 2022-
UpdateFeb 14, 2024-
Current statusFeb 14, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_26863.png

Downloads & links

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Map

FileDownload / File: emd_26863.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTetrahymena telomerase with CST
Voxel sizeX=Y=Z: 1.36 Å
Density
Contour LevelBy AUTHOR: 0.025
Minimum - Maximum-0.1439728 - 0.24749136
Average (Standard dev.)0.00043737332 (±0.0051809466)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 348.16 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_26863_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 1

Fileemd_26863_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_26863_half_map_2.map
Annotationhalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Tetrahymena telomerase holoenzyme

EntireName: Tetrahymena telomerase holoenzyme
Components
  • Complex: Tetrahymena telomerase holoenzyme
    • Protein or peptide: Telomerase La-related protein p65
    • Protein or peptide: Telomerase reverse transcriptase
    • Protein or peptide: Telomerase holoenzyme Teb1 subunit
    • Protein or peptide: Telomerase holoenzyme Teb2 subunit
    • Protein or peptide: Telomerase holoenzyme Teb3 subunit
    • Protein or peptide: Telomerase associated protein p50
    • RNA: Telomerase RNATelomerase RNA component
    • DNA: Telomere DNA
    • Protein or peptide: Telomerase-associated protein of 75 kDa
    • Protein or peptide: Telomerase-associated protein of 19 kDa
    • Protein or peptide: Telomerase-associated protein of 45 kDa
  • Ligand: ZINC ION

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Supramolecule #1: Tetrahymena telomerase holoenzyme

SupramoleculeName: Tetrahymena telomerase holoenzyme / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#11
Source (natural)Organism: Tetrahymena thermophila (eukaryote)

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Macromolecule #1: Telomerase La-related protein p65

MacromoleculeName: Telomerase La-related protein p65 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 64.207363 KDa
SequenceString: MDEYLENTNL EELEQECFME DYQHEDVVEQ ENHQVDANDI YENQQMNDES QLNQDVKISQ QKEQAVEMIE EQQQNNQDKF KQFQDCMAH ITELNFKRNY QNLTEQSSSN NVVAEELDIK ESLKLQMEYY FCDTNLTHDS YLRGIISKSP KNCVDIKVFL K FNKIQQIL ...String:
MDEYLENTNL EELEQECFME DYQHEDVVEQ ENHQVDANDI YENQQMNDES QLNQDVKISQ QKEQAVEMIE EQQQNNQDKF KQFQDCMAH ITELNFKRNY QNLTEQSSSN NVVAEELDIK ESLKLQMEYY FCDTNLTHDS YLRGIISKSP KNCVDIKVFL K FNKIQQIL KQIQDKQIVS TYGIENQSQK KNHKNYKNQN ATFSKKDLIH LIRDSLKESK ILKVKMDSLK VKRRFPFNLE QA LKNSKQR TLYIDFLPPK CSKQTLVSIF GNFRIININL PLQKNSQLCQ GFAFIEFFSE EEANQALITK NSSIPKELIL LTE KKIGQG SIRIITYKKW QEEKQSFKEL SKNQNEQKNK NMNQSRKASD EFVSIDVEIK QNCLIKIINI PQGTLKAEVV LAVR HLGYE FYCDYIDENS NQINSNKISL STQQQNTAQC SNIQIENNLI QQDQHPQLND LLKEGQAMIR FQNSDEQRLA IQKLL NHNN NKLQIEIRGQ ICDVISTIPE DEEKNYWNYI KFKKNEFRKF FFMKKQQKKQ NITQNYNK

UniProtKB: La-related protein 7 homolog

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Macromolecule #2: Telomerase reverse transcriptase

MacromoleculeName: Telomerase reverse transcriptase / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed DNA polymerase
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 133.486938 KDa
SequenceString: MQKINNINNN KQMLTRKEDL LTVLKQISAL KYVSNLYEFL LATEKIVQTS ELDTQFQEFL TTTIIASEQN LVENYKQKYN QPNFSQLTI KQVIDDSIIL LGNKQNYVQQ IGTTTIGFYV EYENINLSRQ TLYSSNFRNL LNIFGEEDFK YFLIDFLVFT K VEQNGYLQ ...String:
MQKINNINNN KQMLTRKEDL LTVLKQISAL KYVSNLYEFL LATEKIVQTS ELDTQFQEFL TTTIIASEQN LVENYKQKYN QPNFSQLTI KQVIDDSIIL LGNKQNYVQQ IGTTTIGFYV EYENINLSRQ TLYSSNFRNL LNIFGEEDFK YFLIDFLVFT K VEQNGYLQ VAGVCLNQYF SVQVKQKKWY KNNFNMNGKA TSNNNQNNAN LSNEKKQENQ YIYPEIQRSQ IFYCNHMGRE PG VFKSSFF NYSEIKKGFQ FKVIQEKLQG RQFINSDKIK PDHPQTIIKK TLLKEYQSKN FSCQEERDLF LEFTEKIVQN FHN INFNYL LKKFCKLPEN YQSLKSQVKQ IVQSENKANQ QSCENLFNSL YDTEISYKQI TNFLRQIIQN CVPNQLLGKK NFKV FLEKL YEFVQMKRFE NQKVLDYICF MDVFDVEWFV DLKNQKFTQK RKYISDKRKI LGDLIVFIIN KIVIPVLRYN FYITE KHKE GSQIFYYRKP IWKLVSKLTI VKLEEENLEK VEEKLIPEDS FQKYPQGKLR IIPKKGSFRP IMTFLRKDKQ KNIKLN LNQ ILMDSQLVFR NLKDMLGQKI GYSVFDNKQI SEKFAQFIEK WKNKGRPQLY YVTLDIKKCY DSIDQMKLLN FFNQSDL IQ DTYFINKYLL FQRNKRPLLQ IQQTNNLNSA MEIEEEKINK KPFKMDNINF PYYFNLKERQ IAYSLYDDDD QILQKGFK E IQSDDRPFIV INQDKPRCIT KDIIHNHLKH ISQYNVISFN KVKFRQKRGI PQGLNISGVL CSFYFGKLEE EYTQFLKNA EQVNGSINLL MRLTDDYLFI SDSQQNALNL IVQLQNCANN NGFMFNDQKI TTNFQFPQED YNLEHFKISV QNECQWIGKS IDMNTLEIK SIQKQTQQEI NQTINVAISI KNLKSQLKNK LRSLFLNQLI DYFNPNINSF EGLCRQLYHH SKATVMKFYP F MTKLFQID LKKSKQYSVQ YGKENTNENF LKDILYYTVE DVCKILCYLQ FEDEINSNIK EIFKNLYSWI MWDIIVSYLK KK KQFKGYL NKLLQKIRKS RFFYLKEGCK SLQLILSQQK YQLNKKELEA IEFIDLNNLI QDIKTLIPKI SAKSNQQNTN

UniProtKB: Telomerase reverse transcriptase

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Macromolecule #3: Telomerase holoenzyme Teb1 subunit

MacromoleculeName: Telomerase holoenzyme Teb1 subunit / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 82.040289 KDa
SequenceString: MKLTKGGSYI LKKVDRKQFY QDEEIVMQIK KILGQKTTDC KQYIKCECID GLGDEALIYF EMLANQNQHL QKNDVIMIQD YLNDKTQND KIVVLVTRFQ FCKASHVQPK TAQKESIQLL NTEKTIIQKS KITKNPAEEV LKFIEVNEKD NSSNSEDMII E QQKQEIKN ...String:
MKLTKGGSYI LKKVDRKQFY QDEEIVMQIK KILGQKTTDC KQYIKCECID GLGDEALIYF EMLANQNQHL QKNDVIMIQD YLNDKTQND KIVVLVTRFQ FCKASHVQPK TAQKESIQLL NTEKTIIQKS KITKNPAEEV LKFIEVNEKD NSSNSEDMII E QQKQEIKN NQKEKQSING FNLEDSYSNI SDITNFGGKS NFNIGSLSDQ LSKQTLLISQ LQVGKNRFSF KFEGRVVYKS ST FQNQQDS KYFFITAQDA NNQEINLSFW QKVDQSYQTL KVGQYYYFIG GEVKQFKNNL ELKFKFGDYQ IIPKETLSAN YVQ PLALQP SKQFGNDSIG DSDYSIHNLI EKEESIAQKG YNGQKNNKYR QNNNNSKHTL LISEVLKTSK QYLSVLAQVV DIQS SDKNI RLKICDNSCN QELKVVIFPD LCYEWRDKFS INKWYYFNEF VRQIYNDEVQ LKNNIHSSIK ESDDQRKVIT YNQEQ GVFK KSISINSNDS FEIKPKISYK NNSNQEQRIY SSIEEIIQQA QASEIGQKKE FYVYGNLVSI QMKNKLYYYR CTCQGK SVL KYHGDSFFCE SCQQFINPQV HLMLRAFVQD STGTIPVMIF DQQSSQLINQ IDPSIHVQEA GQYVKNCIEN GQEEIIR QL FSKLDFARFI FEIQFENKEF NNEQEIAYKV LKIEKENIKE ESKYLLKKLE HLINNNQNN

UniProtKB: Telomeric repeat-binding subunit 1

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Macromolecule #4: Telomerase holoenzyme Teb2 subunit

MacromoleculeName: Telomerase holoenzyme Teb2 subunit / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 30.993035 KDa
SequenceString: MSNRVQGGFD NNSGNNQSAQ KQQAEKIPQI TVPLNCFMIN QIVKAAKENP QAHSGNHYEW YGAFENAIIT AKFEFLQSIN DSPKIMGKL SDSTGCIEVV IQKSKMSDEL PEFVQAYEIE LQNNGNRHKY VRAMLKMRKN AQIQLLYFSI VNDANEISRH G LDLCLRYL ...String:
MSNRVQGGFD NNSGNNQSAQ KQQAEKIPQI TVPLNCFMIN QIVKAAKENP QAHSGNHYEW YGAFENAIIT AKFEFLQSIN DSPKIMGKL SDSTGCIEVV IQKSKMSDEL PEFVQAYEIE LQNNGNRHKY VRAMLKMRKN AQIQLLYFSI VNDANEISRH G LDLCLRYL QRKHGIEDFM HMTNDKAHNN HNASAQKVHY QIDRNQQPKE QVLELMRQIL KHNPNDQIPK SKIIEFFQSQ LN QVQINQI LQQLVSANEI FSVGSDNYLL NV

UniProtKB: Replication protein A 32 kDa subunit

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Macromolecule #5: Telomerase holoenzyme Teb3 subunit

MacromoleculeName: Telomerase holoenzyme Teb3 subunit / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 14.007626 KDa
SequenceString:
MDAEQEQVMY PRILFEQMAQ FRGKKVTVVG NVCNEDQNDS LVIEFGPTGL NQHVVIDNYR RVDLNNTTKF VEIRGVVLNQ NIVSCEELT EFEQKDPFDF DTYSKLIHLS QSDKLSSLFT DQ

UniProtKB: Replication protein A 14 kDa subunit

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Macromolecule #6: Telomerase associated protein p50

MacromoleculeName: Telomerase associated protein p50 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 50.049688 KDa
SequenceString: MKLLLQNQNI FQKLKNTLNG CIKKFYDTYQ DLEQMQKFEM IVEDKLLFRY SCSQSEMFSA QIQAHYLEKR VLQLTDGNVK YIVNFRDKG VLDKANFFDT PNNSLVIIRQ WSYEIYYTKN TFQINLVIDE MRCIDIITTI FYCKLELDFT QGIKGISKSS S FSNQIYEY ...String:
MKLLLQNQNI FQKLKNTLNG CIKKFYDTYQ DLEQMQKFEM IVEDKLLFRY SCSQSEMFSA QIQAHYLEKR VLQLTDGNVK YIVNFRDKG VLDKANFFDT PNNSLVIIRQ WSYEIYYTKN TFQINLVIDE MRCIDIITTI FYCKLELDFT QGIKGISKSS S FSNQIYEY SAQYYKAIQL LKKLLINDSY ISELYNSTKS KQQPRLFIFQ SFKPKMNLAE QNLSRQFEQC QQDDFGDGCL LQ IVNYTHQ SLKQIENKNN SNQIVNGQNE ISKKKRVLKS NEDLYKISLQ KQLKIFQEEE IELHSQSTIR NQTNQQLETF ESD TSKRNS EKILHSINEL NTSKQKVNQM NSSQHQIQKL ENNNLNKNIL NQINENDIKN ELEERQQQHL TQSFNSKAQL KKII TLKKN QDILLFKPQE QEGSKKY

UniProtKB: Telomerase-associated protein of 50 kDa

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Macromolecule #9: Telomerase-associated protein of 75 kDa

MacromoleculeName: Telomerase-associated protein of 75 kDa / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 73.899602 KDa
SequenceString: MEIEEDLNLK ILEDVKKLYL QSFDYIKNGI SSSLPSDKKF LADDDIDLSR ITFLYKFISV NPTLLLINEK TQAKRRIFQG EYLYGKKKI QFNIIAKNLE IERELIQFFK KPYQCYIMHN VQVFQMLNKN KNNNVVEFMD SEDLQSSVDC QLYYLIDESS H VLEDDSMD ...String:
MEIEEDLNLK ILEDVKKLYL QSFDYIKNGI SSSLPSDKKF LADDDIDLSR ITFLYKFISV NPTLLLINEK TQAKRRIFQG EYLYGKKKI QFNIIAKNLE IERELIQFFK KPYQCYIMHN VQVFQMLNKN KNNNVVEFMD SEDLQSSVDC QLYYLIDESS H VLEDDSMD FISTLTRLSD SFNSNEFVFE TNYSIQISQM PKPLNTTHFK LLQPKVVNSF EGVILQVQEG KNILQIEELI DQ VYLNSRR DRFYILKVAN GKNYMDFIEV YLVYDNEDQE AKQQLQFYLK PFQRILIFQS LKHFTKNLKL FMISFFYSSG VQP NNSNVK NFLVSHKGVE FFSRFDIQKN ELLCKDLIKS YNKLPLSNIS KLLEDEGVMI RSNMKFQVRV KKVKYFKIRL NCLN CKQEW TVGLKNCINC KGQQSYISYN IQVLVQDQHF LEQQAYIYLY DDLAAQFFNI TESEKKELHL HLTKNETFIQ LYYSF NKDY PLSIIKFKDK IFNKDITNCI VAYPFADIDN KIFNSQQQII QDENLRIESE KFIQNFTEDN NLQESKLYYE KFKSKN KQQ IFVNGTYIST NYSQGQKICL KPIPCLKVMY VFPQEDIKLS ALKIIEEINQ LKIQIDQLN

UniProtKB: Telomerase-associated protein of 75 kDa

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Macromolecule #10: Telomerase-associated protein of 19 kDa

MacromoleculeName: Telomerase-associated protein of 19 kDa / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 19.498049 KDa
SequenceString:
MQQPKRNFDL YKLITDKQID FQVADLIQDE QSSFVSVRIY GQFKCFVPKS TIQEQLDKIK NLSSKELAKN KIFKFLSEYN KNNQKQDEL SHDYYGYFKV QQHQFILNLE NAQREASLAV DDFYFINGRI YKTNHDILIL QAHHVYQMQK PTLQLLQAAS E INQN

UniProtKB: Telomerase-associated protein of 19 kDa

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Macromolecule #11: Telomerase-associated protein of 45 kDa

MacromoleculeName: Telomerase-associated protein of 45 kDa / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 43.682938 KDa
SequenceString: MEDNFELVFL KELPSLPDFS KVCFTGLILS FSNFPSSEQN QQKDVPHKIA IIQDSTGEAE LFLDMYKFCQ EEISVFKAIT GIGVLKKKN IGAGQVCKII VERFRIIHSA DEEMLQYLLI QKYKLSKTLN EQQQIKQKEQ QINQQKIDKV VQDKESKEHL L WKQQQIPQ ...String:
MEDNFELVFL KELPSLPDFS KVCFTGLILS FSNFPSSEQN QQKDVPHKIA IIQDSTGEAE LFLDMYKFCQ EEISVFKAIT GIGVLKKKN IGAGQVCKII VERFRIIHSA DEEMLQYLLI QKYKLSKTLN EQQQIKQKEQ QINQQKIDKV VQDKESKEHL L WKQQQIPQ IKSNQENINT LKYKELIAGE LMRITHKLLI QKLQQQQPAN NNKQINEMDV ESNELAEKKE VIIKIQEIAK DQ QLYDTLS IQYQVDQKEQ YYAKIAQSLE DFVSISALKM VSYIYPNISY QVSIGFFQNI LDIATKTVKD RGALGCNYKY LKD KLTKAL NLQQISYPLI SESYISYLVH LFQDFNIIEI ENEHKFYYKQ AFQYDDS

UniProtKB: Telomerase-associated protein of 45 kDa

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Macromolecule #7: Telomerase RNA

MacromoleculeName: Telomerase RNA / type: rna / ID: 7 / Number of copies: 1
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 50.746984 KDa
SequenceString:
AUACCCGCUU AAUUCAUUCA GAUCUGUAAU AGAACUGUCA UUCAACCCCA AAAAUCUAGU GCUGAUAUAA CCUUCACCAA UUAGGUUCA AAUAAGUGGU AAUGCGGGAC AAAAGACUAU CGACAUUUGA UACACUAUUU AUCAAUGGAU GUCUUAUUUU

GENBANK: GENBANK: AF399707.1

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Macromolecule #8: Telomere DNA

MacromoleculeName: Telomere DNA / type: dna / ID: 8 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 9.581087 KDa
SequenceString:
(DG)(DT)(DT)(DG)(DG)(DG)(DG)(DT)(DT)(DG) (DG)(DG)(DG)(DT)(DT)(DG)(DG)(DG)(DG)(DT) (DT)(DG)(DG)(DG)(DG)(DT)(DT)(DG)(DG) (DG)

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Macromolecule #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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 TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 4.0 µm / Nominal defocus min: 0.8 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 48.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

23437

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 259330
FSC plot (resolution estimation)

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Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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