Evidence map›Paper›PMID 20399182›Full record

ArticleStructure (London, England : 1993)2010

Structure of the RNA 3'-phosphate cyclase-adenylate intermediate illuminates nucleotide specificity and covalent nucleotidyl transfer.

Naoko Tanaka, Paul Smith, Stewart Shuman

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Archaeal 3'-phosphate RNA splicing ligase characterization identifies the missing component in tRNA maturation.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

3 authors at 1 institution in 1 country.

Naoko TanakaMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Paul Smith
Stewart Shuman
Kettering University · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Vaccina Virus DNA TopoisomeraseR37GM046330 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI SHUMAN, STEWART H · 2007 to 2016
$6.1M
VACCINIA VIRUS DNA TOPOISOMERASE IR01GM046330 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 1991 to 2006
$3.1M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM46330NIGMS NIH HHS R01 GM046330NIGMS NIH HHS R37 GM046330
6 · The paper itself

Abstract

RNA 3'-phosphate cyclase (RtcA) synthesizes RNA 2',3' cyclic phosphate ends via three steps: reaction with ATP to form a covalent RtcA-AMP intermediate; transfer of adenylate to an RNA 3'-phosphate to form RNA(3')pp(5')A; and attack of the vicinal O2' on the 3'-phosphorus to form a 2',3' cyclic phosphate. Here we report the 1.7 A crystal structure of the RtcA-AMP intermediate, which reveals the mechanism of nucleotidyl transfer. Adenylate is linked via a phosphoamide bond to the His309 Nepsilon atom. A network of hydrogen bonds to the ribose O2' and O3' accounts for the stringent ribonucleotide preference. Adenine is sandwiched in a hydrophobic pocket between Tyr284 and Pro131 and the preference for adenine is enforced by Phe135, which packs against the purine C2 edge. Two sulfates bound near the adenylate plausibly mimic the 3'-terminal and penultimate phosphates of RNA. The structure illuminates how the four alpha2/beta4 domains contribute to substrate binding and catalysis.

Indexed as

AdenineAnionsCatalysisCatalytic DomainCrystallography, X-RayEscherichia coliHistidineLigasesMolecular ConformationMutagenesisNucleotidesPhosphorusProtein BindingProtein ConformationPurinesRNAAdenineAnionsHistidineLigasesNucleotidesPhosphoruspurinePurinesRNARNA 3'-terminal phosphate cyclase2’,3’ cyclic phosphodiesteradenylyltransferasecovalent catalysisRNA processing

Identifiers

PMID20399182
PMCPMC2858066
OpenAlexW1981143847

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.