Evidence map›Paper›PMID 19279186›Full record

ArticleNucleic acids research2009

A recurrent magnesium-binding motif provides a framework for the ribosomal peptidyl transferase center.

Chiaolong Hsiao, Loren Dean Williams

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 71 citations in OpenAlex.

  1. The master molecule that built biology: How water shaped the chemistry of life.Protein science : a publication of the Protein Society · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Peptidyl Transferase Center: a Window to the Past.Microbiology and molecular biology reviews : MMBR · 2021
    Article
  7. Review
  8. An uncommon [KRNA (New York, N.Y.) · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Piece by piece: Building a ribozyme.The Journal of biological chemistry · 2020
    Review
  13. Prebiotic Iron Originates the Peptidyl Transfer Origin.Molecular biology and evolution · 2019
    Article
  14. Nucleobase carbonyl groups are poor MgRNA (New York, N.Y.) · 2019
    Article
  15. Multiple prebiotic metals mediate translation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. The ribosome challenge to the RNA world.Journal of molecular evolution · 2015
    Review
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

2 authors at 1 institution in 1 country.

Chiaolong HsiaoSchool of Chemistry and Biochemistry, Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0400, USA.
Loren Dean Williams
Georgia Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribosome is an ancient macromolecular machine responsible for the synthesis of all proteins in all living organisms. Here we demonstrate that the ribosomal peptidyl transferase center (PTC) is supported by a framework of magnesium microclusters (Mg(2+)-muc's). Common features of Mg(2+)-muc's include two paired Mg(2+) ions that are chelated by a common bridging phosphate group in the form Mg((a))(2+)-(O1P-P-O2P)-Mg((b))(2+). This bridging phosphate is part of a 10-membered chelation ring in the form Mg((a))(2+)-(OP-P-O5'-C5'-C4'-C3'-O3'-P-OP)-Mg((a))(2+). The two phosphate groups of this 10-membered ring are contributed by adjacent residues along the RNA backbone. Both Mg(2+) ions are octahedrally coordinated, but are substantially dehydrated by interactions with additional RNA phosphate groups. The Mg(2+)-muc's in the LSU (large subunit) appear to be highly conserved over evolution, since they are unchanged in bacteria (Thermus thermophilus, PDB entry 2J01) and archaea (Haloarcula marismortui, PDB entry 1JJ2). The 2D elements of the 23S rRNA that are linked by Mg(2+)-muc's are conserved between the rRNAs of bacteria, archaea and eukarya and in mitochondrial rRNA, and in a proposed minimal 23S-rRNA. We observe Mg(2+)-muc's in other rRNAs including the bacterial 16S rRNA, and the P4-P6 domain of the tetrahymena Group I intron ribozyme. It appears that Mg(2+)-muc's are a primeval motif, with pivotal roles in RNA folding, function and evolution.

Indexed as

Binding SitesHaloarcula marismortuiMagnesiumModels, MolecularNucleic Acid ConformationPeptidyl TransferasesPhosphatesRibosomal ProteinsRibosomesRibosome Subunits, Large, ArchaealRibosome Subunits, Large, BacterialRNA, RibosomalThermus thermophilusMagnesiumPeptidyl TransferasesPhosphatesRibosomal ProteinsRNA, Ribosomal

Identifiers

PMID19279186
PMCPMC2691814
OpenAlexW2032607419

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.