Evidence map›Paper›PMID 19666563›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structural organization of box C/D RNA-guided RNA methyltransferase.

Keqiong Ye, Ru Jia, Jinzhong Lin, Minghua Ju, Jin Peng, Anbi Xu, Liman Zhang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

42 citing papers in PubMed, 65 citations in OpenAlex.

  1. A sequence-specific RNA acetylation catalyst.Nucleic acids research · 2025
    Article
  2. Article
  3. A sequence-specific RNA acetylation catalyst.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Advances in the structure and function of the nucleolar protein fibrillarin.Frontiers in cell and developmental biology · 2024
    Review
  6. On the origin of the nucleus: a hypothesis.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  7. Review
  8. The roles of NOP56 in cancer and SCA36.Pathology oncology research : POR · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Box C/D guide RNAs recognize a maximum of 10 nt of substrates.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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

7 authors at 2 institutions in 1 country.

Keqiong YeNational Institute of Biological Sciences, Beijing 102206, China.
Ru Jia
Jinzhong Lin
Minghua Ju
Jin Peng
Anbi Xu
Liman Zhang
National Institute of Biological Sciences, Beijing · CNChinese Academy of Medical Sciences & Peking Union Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Box C/D guide RNAs are abundant noncoding RNAs that primarily function to direct the 2'-O-methylation of specific nucleotides by base-pairing with substrate RNAs. In archaea, a bipartite C/D RNA assembles with L7Ae, Nop5, and the methyltransferase fibrillarin into a modification enzyme with unique substrate specificity. Here, we determined the crystal structure of an archaeal C/D RNA-protein complex (RNP) composed of all 3 core proteins and an engineered half-guide RNA at 4 A resolution, as well as 2 protein substructures at higher resolution. The RNP structure reveals that the C-terminal domains of Nop5 in the dimeric complex provide symmetric anchoring sites for 2 L7Ae-associated kink-turn motifs of the C/D RNA. A prominent protrusion in Nop5 seems to be important for guide RNA organization and function and for discriminating the structurally related U4 snRNA. Multiple conformations of the N-terminal domain of Nop5 and its associated fibrillarin in different structures indicate the inherent flexibility of the catalytic module, suggesting that a swinging motion of the catalytic module is part of the enzyme mechanism. We also built a model of a native C/D RNP with substrate and fibrillarin in an active conformation. Our results provide insight into the overall organization and mechanism of action of C/D RNA-guided RNA methyltransferases.

Indexed as

Amino Acid MotifsArchaeal ProteinsBase SequenceCarrier ProteinsCatalysisChromosomal Proteins, Non-HistoneCrystallography, X-RayMolecular ConformationMolecular Sequence DataNucleic Acid ConformationProtein EngineeringProtein Structure, SecondaryProtein Structure, TertiaryRNARNA, ArchaealtRNA MethyltransferasesArchaeal ProteinsCarrier ProteinsChromosomal Proteins, Non-HistonefibrillarinRNARNA, ArchaealtRNA Methyltransferases

Identifiers

PMID19666563
PMCPMC2728976
OpenAlexW2099855129

What OpenQuestion holds

Textmetadata
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.