[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

TitleStructure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.
Journal, issue, pagesScience, Vol. 350, Issue 6260, Page aab4070, Year 2015
Publish dateOct 30, 2015
AuthorsJiansen Jiang / Henry Chan / Darian D Cash / Edward J Miracco / Rachel R Ogorzalek Loo / Heather E Upton / Duilio Cascio / Reid O'Brien Johnson / Kathleen Collins / Joseph A Loo / Z Hong Zhou / Juli Feigon /
PubMed AbstractTelomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the ...Telomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protein A (RPA). The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1). This study reveals the paths of TER in the TERT-TER-p65 catalytic core and single-stranded DNA exit; extensive subunit interactions of the TERT essential N-terminal domain, p50, and TEB; and other subunit identities and structures, including p19 and p45C crystal structures. Our findings provide structural and mechanistic insights into telomerase holoenzyme function.
External linksScience / PubMed:26472759 / PubMed Central
MethodsEM (single particle) / X-ray diffraction / NMR (solution)
Resolution2.301 - 9.4 Å
Structure data

EMDB-6442:
CryoEM structure of endogenously assembled Tetrahymena telomerase holoenzyme at 9.4 Angstrom resolution
Method: EM (single particle) / Resolution: 9.4 Å

EMDB-6443:
CryoEM structure of endogenously assembled Tetrahymena telomerase holoenzyme at 8.9 Angstrom resolution
Method: EM (single particle) / Resolution: 8.9 Å

PDB-5dfm:
Structure of Tetrahymena telomerase p19 fused to MBP
Method: X-RAY DIFFRACTION / Resolution: 2.301 Å

PDB-5dfn:
Structure of Tetrahymena Telomerase P45 C-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 2.382 Å

PDB-5kmz:
Solution NMR structure of Tetrahymena telomerase RNA pseudoknot
Method: SOLUTION NMR

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • tetrahymena thermophila (eukaryote)
  • escherichia coli (E. coli)
KeywordsNUCLEAR PROTEIN / Telomerase / P19 / CST complex / Ten1 / OB-fold / Oligonucleotide Binding Fold / P45 / Stn1 / Winged Helix / WH domain / WHtH / Winged Helix turn Helix / RNA / pseudoknot / triplex

+
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