[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleCryo-EM structure of human telomerase dimer reveals H/ACA RNP-mediated dimerization.
Journal, issue, pagesScience, Vol. 389, Issue 6756, Page eadr5817, Year 2025
Publish dateJul 10, 2025
AuthorsSebastian Balch / Zala Sekne / Elsa Franco-Echevarría / Patryk Ludzia / Rachael C Kretsch / Wenqing Sun / Haopeng Yu / George E Ghanim / Sigurdur Thorkelsson / Yiliang Ding / Rhiju Das / Thi Hoang Duong Nguyen /
PubMed AbstractTelomerase ribonucleoprotein (RNP) synthesizes telomeric repeats at chromosome ends using a telomerase reverse transcriptase (TERT) and a telomerase RNA (hTR in humans). Previous structural work ...Telomerase ribonucleoprotein (RNP) synthesizes telomeric repeats at chromosome ends using a telomerase reverse transcriptase (TERT) and a telomerase RNA (hTR in humans). Previous structural work showed that human telomerase is typically monomeric, containing a single copy of TERT and hTR. Evidence for dimeric complexes exists, although the composition, high-resolution structure, and function remain elusive. Here, we report the cryo-electron microscopy (cryo-EM) structure of a human telomerase dimer bound to telomeric DNA. The structure reveals a 26-subunit assembly and a dimerization interface mediated by the Hinge and ACA box (H/ACA) RNP of telomerase. Premature aging disease mutations map to this interface. Disrupting dimer formation affects RNP assembly, bulk telomerase activity, and telomere maintenance in cells. Our findings address a long-standing enigma surrounding the telomerase dimer and suggest a role for the dimer in telomerase assembly.
External linksScience / PubMed:40638752 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 6.2 Å
Structure data

EMDB-52976: Consensus dimer structure of human telomerase
Method: EM (single particle) / Resolution: 6.2 Å

52978

9qax

EMDB-52978, PDB-9qax:
The catalytic core with C2 symmetry of human telomerase dimer
Method: EM (single particle) / Resolution: 3.3 Å

52979

9qay

EMDB-52979, PDB-9qay:
Catalytic core 1 of dimeric human telomerase
Method: EM (single particle) / Resolution: 3.8 Å

52980

9qaz

EMDB-52980, PDB-9qaz:
Catalytic core 2 of dimeric human telomerase
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-52981: Catalytic core 1 of human telomerase dimer from particles common to both catalytic cores of the dimer
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-52982: Catalytic core 2 of the telomerase dimer with common particles to both catalytic cores of the dimer
Method: EM (single particle) / Resolution: 3.9 Å

52983

9qb2

EMDB-52983, PDB-9qb2:
H/ACA RNP protomer of human telomerase dimer
Method: EM (single particle) / Resolution: 3.0 Å

52984

9qb3

EMDB-52984, PDB-9qb3:
Dimer structure of H/ACA RNP lobe of human telomerase
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / telomerase / H/ACA / DNA BINDING PROTEIN / Human telomerase catalytic core / reverse transcriptase / DNA substrate bound / RNA-binding protein

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more