Evidence map›Paper›PMID 27762343›Full record

ArticleScientific reports2016

Cryo-EM structure of the large subunit of the spinach chloroplast ribosome.

Tofayel Ahmed, Zhan Yin, Shashi Bhushan

Abstract read
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Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
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25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Diversification of Plastid Structure and Function in Land Plants.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Review
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  15. Real-space refinement in PHENIX for cryo-EM and crystallography.Acta crystallographica. Section D, Structural biology · 2018
    Article
  16. Review
  17. Article
  18. Article
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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Tofayel AhmedSchool of Biological Sciences, Nanyang Technological University, Singapore.
Zhan YinSchool of Biological Sciences, Nanyang Technological University, Singapore.
Shashi BhushanSchool of Biological Sciences, Nanyang Technological University, Singapore.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein synthesis in the chloroplast is mediated by the chloroplast ribosome (chloro-ribosome). Overall architecture of the chloro-ribosome is considerably similar to the Escherichia coli (E. coli) ribosome but certain differences are evident. The chloro-ribosome proteins are generally larger because of the presence of chloroplast-specific extensions in their N- and C-termini. The chloro-ribosome harbours six plastid-specific ribosomal proteins (PSRPs); four in the small subunit and two in the large subunit. Deletions and insertions occur throughout the rRNA sequence of the chloro-ribosome (except for the conserved peptidyl transferase center region) but the overall length of the rRNAs do not change significantly, compared to the E. coli. Although, recent advancements in cryo-electron microscopy (cryo-EM) have provided detailed high-resolution structures of ribosomes from many different sources, a high-resolution structure of the chloro-ribosome is still lacking. Here, we present a cryo-EM structure of the large subunit of the chloro-ribosome from spinach (Spinacia oleracea) at an average resolution of 3.5 Å. High-resolution map enabled us to localize and model chloro-ribosome proteins, chloroplast-specific protein extensions, two PSRPs (PSRP5 and 6) and three rRNA molecules present in the chloro-ribosome. Although comparable to E. coli, the polypeptide tunnel and the tunnel exit site show chloroplast-specific features.

Indexed as

Cryoelectron MicroscopyChloroplastsRibosome Subunits, LargeSpinacia oleracea

Identifiers

PMID27762343
PMCPMC5071890

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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.