Evidence map›Paper›PMID 28007896›Full record

ArticleThe EMBO journal2017

The complete structure of the chloroplast 70S ribosome in complex with translation factor pY.

Philipp Bieri, Marc Leibundgut, Martin Saurer, Daniel Boehringer, Nenad Ban

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
11.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

97 citing papers in PubMed, 1 synthesis or guideline pooled it, 160 citations in OpenAlex.

  1. Pooled it
  2. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. RNA regulation in plants.Science China. Life sciences · 2026
    Review
  6. RiboScreenBiomedicines · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Plant MutS2 proteins function in plastid ribosome quality control.bioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

37 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Philipp BieriDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Marc LeibundgutDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Martin SaurerDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Daniel BoehringerDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Nenad BanDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland ban@mol.biol.ethz.ch.ORCID 0000-0002-9527-210X
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplasts are cellular organelles of plants and algae that are responsible for energy conversion and carbon fixation by the photosynthetic reaction. As a consequence of their endosymbiotic origin, they still contain their own genome and the machinery for protein biosynthesis. Here, we present the atomic structure of the chloroplast 70S ribosome prepared from spinach leaves and resolved by cryo-EM at 3.4 Å resolution. The complete structure reveals the features of the 4.5S rRNA, which probably evolved by the fragmentation of the 23S rRNA, and all five plastid-specific ribosomal proteins. These proteins, required for proper assembly and function of the chloroplast translation machinery, bind and stabilize rRNA including regions that only exist in the chloroplast ribosome. Furthermore, the structure reveals plastid-specific extensions of ribosomal proteins that extensively remodel the mRNA entry and exit site on the small subunit as well as the polypeptide tunnel exit and the putative binding site of the signal recognition particle on the large subunit. The translation factor pY, involved in light- and temperature-dependent control of protein synthesis, is bound to the mRNA channel of the small subunit and interacts with 16S rRNA nucleotides at the A-site and P-site, where it protects the decoding centre and inhibits translation by preventing tRNA binding. The small subunit is locked by pY in a non-rotated state, in which the intersubunit bridges to the large subunit are stabilized.

Indexed as

ChloroplastsSpinacia oleraceaCryoelectron MicroscopyModels, MolecularRibosomal ProteinsRibosomesRNA, RibosomalRibosomal ProteinsRNA, Ribosomalchloroplastcryo‐EMpYribosometranslation

Identifiers

PMID28007896
PMCPMC5694952
OpenAlexW2562045321

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.