Evidence map›Paper›PMID 21076397›Full record

ArticleNature2010

Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA.

Nicholas J Reiter, Amy Osterman, Alfredo Torres-Larios, Kerren K Swinger, Tao Pan, Alfonso Mondragón

Open access · greenAbstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers.

0numbers the graph read from it
0cells of the map it votes in
195citing papers in PubMed
9.6field-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

195 citing papers in PubMed, 296 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026
    Article
  6. Article
  7. Coevolution of RNase P and the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026
    Article
  9. Article
  10. Article
  11. Structural insights into higher-order natural RNA-only multimers.Nature structural & molecular biology · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Molecular determinants of RNase MRP specificity and function.bioRxiv : the preprint server for biology · 2025
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Nicholas J ReiterDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.
Amy Osterman
Alfredo Torres-Larios
Kerren K Swinger
Tao Pan
Alfonso Mondragón
Northwestern University · USUniversidad Nacional Autónoma de México · MXUniversity of Chicago · US

Funding

STRUCTURAL STUDIES OF THE RNA COMPONENT OF RNASE PR01GM058443 · NIGMS · NORTHWESTERN UNIVERSITY · PI MONDRAGON, ALFONSO · 1999 to 2015
$3.8M
Structure and Function of an RNase P ribonucleoprotein-tRNA ternary complexF32GM087055 · NIGMS · NORTHWESTERN UNIVERSITY · PI REITER, NICHOLAS J · 2009 to 2011
$157k
NIGMS NIH HHS F32 GM087055NIGMS NIH HHS R01 GM058443
6 · The paper itself

Abstract

Ribonuclease (RNase) P is the universal ribozyme responsible for 5'-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNA(Phe). The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA-RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5' leader sequence with and without metal help to identify the 5' substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P-tRNA contacts suggest a universal mechanism of catalysis by RNase P.

Indexed as

BiocatalysisCatalytic DomainCrystallography, X-RayGenes, BacterialHoloenzymesMetalsModels, MolecularMolecular ConformationRibonuclease PRNA, Transfer, PheStructure-Activity RelationshipSubstrate SpecificityThermotoga maritimaHoloenzymesMetalsRibonuclease PRNA, Transfer, Phe

Identifiers

PMID21076397
PMCPMC3058908
OpenAlexW1986221874

What OpenQuestion holds

Textmetadata
LicenceTDM
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.