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- EMDB-55322: The catalytic core of yeast telomerase holoenzyme -

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Basic information

Entry
Database: EMDB / ID: EMD-55322
TitleThe catalytic core of yeast telomerase holoenzyme
Map dataPost-processed map
Sample
  • Complex: The catalytic core of yeast telomerase holoenzyme
    • Complex: Yeast telomerase catalytic core
      • RNA: TLC1 RNA
      • Protein or peptide: Telomerase reverse transcriptase
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
KeywordsTelomerase / Telomerase RNA / RNA BINDING PROTEIN
Function / homology
Function and homology information


telomerase catalytic core complex / telomerase activity / telomerase holoenzyme complex / telomerase RNA binding / telomeric repeat DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / chromosome, telomeric region / nucleolus / metal ion binding / nucleus
Similarity search - Function
Telomerase ribonucleoprotein complex - RNA binding domain / Telomerase reverse transcriptase / Telomerase ribonucleoprotein complex - RNA-binding domain / Telomerase ribonucleoprotein complex - RNA binding domain / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile.
Similarity search - Domain/homology
Telomerase reverse transcriptase
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsHu H / Franco-Echevarria E / Nguyen THD / Ahsan B / Oluwole A / Peak-Chew S / Robinson CV
Funding support United Kingdom, European Union, 2 items
OrganizationGrant numberCountry
UK Research and Innovation (UKRI)MC_UP_1201/19 United Kingdom
European Molecular Biology Organization (EMBO)European Union
CitationJournal: Science / Year: 2026
Title: Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.
Authors: Hongmiao Hu / Hannah Neumann / Gabriela M Teplitz / Elsa Franco-Echevarría / Pascal Chartrand / Raymund J Wellinger / Thi Hoang Duong Nguyen /
Abstract: Telomerase is a reverse transcriptase that synthesizes telomeric repeats at chromosome ends, safeguarding genome integrity. We present the cryo-electron microscopy structure of the budding yeast ...Telomerase is a reverse transcriptase that synthesizes telomeric repeats at chromosome ends, safeguarding genome integrity. We present the cryo-electron microscopy structure of the budding yeast telomerase, which exhibits substantial divergence from its ciliate and vertebrate counterparts. The structure reveals a stable core formed by telomerase RNA TLC1; the three ever shorter telomere (Est) proteins, Est1, Est2 and Est3; and the Pop1/Pop6/Pop7 complex (Pop1/6/7). TLC1, Est3, and Pop1/6/7 serve critical roles in complex assembly. We identified a zinc finger (ZnF) motif in the telomerase reverse transcriptase (TERT) subunit Est2 that is crucial for telomerase function. Structure prediction suggests the presence of ZnFs in TERT from diverse species. These findings offer insights into the functional organization of yeast telomerase and underscore the evolutionary diversity of telomerase holoenzymes.
History
DepositionOct 7, 2025-
Header (metadata) releaseApr 8, 2026-
Map releaseApr 8, 2026-
UpdateApr 8, 2026-
Current statusApr 8, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_55322.png

Downloads & links

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Map

FileDownload / File: emd_55322.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPost-processed map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.96 Å/pix.
x 360 pix.
= 343.8 Å		0.96 Å/pix.
x 360 pix.
= 343.8 Å		0.96 Å/pix.
x 360 pix.
= 343.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.955 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.71369445 - 1.3020536
Average (Standard dev.)0.0033682934 (±0.022856101)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 343.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_55322_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Local refinement of the catalytic core, half-map

Fileemd_55322_half_map_1.map
AnnotationLocal refinement of the catalytic core, half-map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Local refinement of the catalytic core, half-map

Fileemd_55322_half_map_2.map
AnnotationLocal refinement of the catalytic core, half-map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : The catalytic core of yeast telomerase holoenzyme

EntireName: The catalytic core of yeast telomerase holoenzyme
Components
  • Complex: The catalytic core of yeast telomerase holoenzyme
    • Complex: Yeast telomerase catalytic core
      • RNA: TLC1 RNA
      • Protein or peptide: Telomerase reverse transcriptase
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION

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Supramolecule #1: The catalytic core of yeast telomerase holoenzyme

SupramoleculeName: The catalytic core of yeast telomerase holoenzyme / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #2: Yeast telomerase catalytic core

SupramoleculeName: Yeast telomerase catalytic core / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2
Details: Yeast telomerase catalytic core consists of protein component Est2 and RNA component TLC1
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: TLC1 RNA

MacromoleculeName: TLC1 RNA / type: rna / ID: 1 / Number of copies: 1
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 370.246406 KDa
SequenceString: GAGAGGAAGA UAGGUACCCU AUGAAAAUGU CAAUGGCUGU UGCGUUUGCU UAAUCGUAUU UUUUUUUUUU UCAGUCCGUG UUUUUUGUA CAUUCUACGU UUGAGUUUUC CAUCAUGCAG GCCUCAGAAA UUUGGUAGGC ACUCGAUGGU GAAGAGAUAG U GUCGGAUU ...String:
GAGAGGAAGA UAGGUACCCU AUGAAAAUGU CAAUGGCUGU UGCGUUUGCU UAAUCGUAUU UUUUUUUUUU UCAGUCCGUG UUUUUUGUA CAUUCUACGU UUGAGUUUUC CAUCAUGCAG GCCUCAGAAA UUUGGUAGGC ACUCGAUGGU GAAGAGAUAG U GUCGGAUU UCGGAUUGAU CUUUCAGUUG AUAGCCUGCU GCUCUUUUCU UUUCCAAAGA AUUUCGAGUA UGCUGGUGUC AG UGUAGAU GCUUGUGUGU GCGCAAUUUG UGGUUUUUUA UUGUGUUUCU ACUUAUAGAU GGCUAAAAUC UGAGUUUAGA AAA UGCAAA CCGUAAAUUC UUAAACACUG CUAUUGCAUU UAGUUGCUAA AGCAGUGUUU UUGAACUUAU UCCUGUUAUU CCUU CUUCG UACCGAUCCU CUUCUCGACC UAACCUUUUA AUUACCAUGG GAAGCCUACC AUCACCACAC CCACACACAA AUGUU ACAG CUAAUUGUUU AUUAGCAAAG UUUGCACGAG UUCGCUGUUU AUUUUUUUCU CGUUUUCUUA UACCUAGUAU UUUUUC UGA CACUGUUUAA GGUGACAGAA AAAAAGGAGU UUAAGUUAGA UUUGCAAACA GACGGUGCUA AGCGCUGUCA CUUUAUG UC UAUCUUAUCG UUAACUCUGG AAAAAGAAAA AGGAAAAAGA ACGUCAGGGA ACAUGAGUAU AUAUAGAAAU GGUUUAUU C UAGUUUUUUC CGUUUUUUCA GUAGAUUUUU GCCUUUAAAA GAAUAAAUCC CACUACAAAA AGGUAAAAUA AAAAAUCUA UUCACUGAAC UUACUGAUGA AAUUUCCAAA UGUGCCCCGU ACAUCGAACG AUGUGACAGA GAAAAAUACG AGUAGGUAAA UAAGCCAAA AGGCAAGGGU GUCCUUUCUU AAGCAUCGGU UAGGUUUGCG GGCGAUCAGU AACUGAACAA UGACACAAGA U CAAGAACG UAAUUUGAGA UUUUUCAAGA UGGUUUUUUU AGGUAUCUAU UAAAACUACU UUGAUGAUCA AUACGGUAUU UU UGUCGCA UUAUUUUCCA AGCGGAAGGA ACCGUGUGUU CAUUUUAUGA AUCUUGGUGU UGUAUUCACA GCUACUUCUC CUA AUGCCU UCGAUGCAUU UAGAUAAUUU UUGGAAACAU U

GENBANK: GENBANK: U14595.1

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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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 102.768094 KDa
SequenceString: MKILFEFIQD KLDIDLQTNS TYKENLKCGH FNGLDEILTT CFALPNSRKI ALPCLPGDLS HKAVIDHCII YLLTGELYNN VLTFGYKIA RNEDVNNSLF CHSANVNVTL LKGAAWKMFH SLVGTYAFVD LLINYTVIQF NGQFFTQIVG NRCNEPHLPP K WAQRSSSS ...String:
MKILFEFIQD KLDIDLQTNS TYKENLKCGH FNGLDEILTT CFALPNSRKI ALPCLPGDLS HKAVIDHCII YLLTGELYNN VLTFGYKIA RNEDVNNSLF CHSANVNVTL LKGAAWKMFH SLVGTYAFVD LLINYTVIQF NGQFFTQIVG NRCNEPHLPP K WAQRSSSS SATAAQIKQL TEPVTNKQFL HKLNINSSSF FPYSKILPSS SSIKKLTDLR EAIFPTNLVK IPQRLKVRIN LT LQKLLKR HKRLNYVSIL NSICPPLEGT VLDLSHLSRQ SPKERVLKFI IVILQKLLPQ EMFGSKKNKG KIIKNLNLLL SLP LNGYLP FDSLLKKLRL KDFRWLFISD IWFTKHNFEN LNQLAICFIS WLFRQLIPKI IQTFFYCTEI SSTVTIVYFR HDTW NKLIT PFIVEYFKTY LVENNVCRNH NSYTLSNFNH SKMRIIPKKS NNEFRIIAIP CRGADEEEFT IYKENHKNAI QPTQK ILEY LRNKRPTSFT KIYSPTQIAD RIKEFKQRLL KKFNNVLPEL YFMKFDVKSC YDSIPRMECM RILKDALKNE NGFFVR SQY FFNTNTGVLK LFNVVNASRV PKPYELYIDN VRTVHLSNQD VINVVEMEIF KTALWVEDKC YIREDGLFQG SSLSAPI VD LVYDDLLEFY SEFKASPSQD TLILKLADDF LIISTDQQQV INIKKLAMGG FQKYNAKANR DKILAVSSQS DDDTVIQF C AMHIFVKELE VWKHSSTMNN FHIRSKSSKG IFRSLIALFN TRISYKTIDT NLNSTNTVLM QIDHVVKNIS ECYKSAFKD LSINVTQNMQ FHSFLQRIIE MTVSGCPITK CDPLIEYEVR FTILNGFLES LSSNTSKFKD NIILLRKEIQ HLQAYIYIYI HIVN

UniProtKB: Telomerase reverse transcriptase

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #4: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 4 / Number of copies: 1 / 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
Component:
ConcentrationFormulaName
150.0 mMNaClSodium chloride
20.0 mMC8H18N2O4SHEPES
2.0 mMMgCl2Magnesium chloride
1.0 %C3H8O3glycerol
0.05 %(C2H4O)nC14H22OIgepal CA-630
1.0 mMC4H10O2S2Dithiothreitol
0.2 mMC7H7FO2SPhenylmethanesulfonyl fluoride

Details: 150 mM NaCl, 20 mM HEPES NaOH pH 8.0, 2 mM MgCl2, 1% glycerol, 0.05% IGEPAL CA-630, 1 mM DTT, 0.2 mM PMSF
GridModel: UltrAuFoil R1.2/1.3 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV / Details: Blot Force: 10 Blot Time: 7.0 s Wait Time: 5 min.

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Electron microscopy

MicroscopeTFS KRIOS
TemperatureMin: 78.0 K
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 24936 / Average exposure time: 4.4 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 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

DetailsImages were processed using RELION5.0 and cryoSPARC
Particle selectionNumber selected: 1876851
CTF correctionSoftware - Name: CTFFIND / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.5) / Number images used: 125104
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 4.5)
FSC plot (resolution estimation)

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