Evidence map›Paper›PMID 17488874›Full record

ArticleRNA (New York, N.Y.)2007

A comparison of vanadate to a 2'-5' linkage at the active site of a small ribozyme suggests a role for water in transition-state stabilization.

Andrew T Torelli, Jolanta Krucinska, Joseph E Wedekind

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Investigation of the pThe journal of physical chemistry. B · 2021
    Article
  3. Crucial Roles of Two Hydrated MgAngewandte Chemie (International ed. in English) · 2020
    Article
  4. Article
  5. Strand-specific (asymmetric) contribution of phosphodiester linkages on RNA polymerase II transcriptional efficiency and fidelity.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. Article
  7. Article
  8. Article
  9. Crystallographic analysis of small ribozymes and riboswitches.Methods in molecular biology (Clifton, N.J.) · 2012
    Article
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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 2 institutions in 1 country.

Andrew T TorelliDepartment of Biochemistry and Biophysics, Rochester, NY 14642, USA.
Jolanta Krucinska
Joseph E Wedekind
University of Rochester · USApplied BioPhysics (United States) · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
Mechanisms of Action On Non-Coding RNA MoleculesR01GM063162 · NIGMS · UNIVERSITY OF ROCHESTER · PI WEDEKIND, JOSEPH E · 2001 to 2024
$6.8M
NCRR NIH HHS P41 RR001209NIGMS NIH HHS R01 GM063162NIGMS NIH HHS R01 GM63162
6 · The paper itself

Abstract

The potential for water to participate in RNA catalyzed reactions has been the topic of several recent studies. Here, we report crystals of a minimal, hinged hairpin ribozyme in complex with the transition-state analog vanadate at 2.05 A resolution. Waters are present in the active site and are discussed in light of existing views of catalytic strategies employed by the hairpin ribozyme. A second structure harboring a 2',5'-phosphodiester linkage at the site of cleavage was also solved at 2.35 A resolution and corroborates the assignment of active site waters in the structure containing vanadate. A comparison of the two structures reveals that the 2',5' structure adopts a conformation that resembles the reaction intermediate in terms of (1) the positioning of its nonbridging oxygens and (2) the covalent attachment of the 2'-O nucleophile with the scissile G+1 phosphorus. The 2',5'-linked structure was then overlaid with scissile bonds of other small ribozymes including the glmS metabolite-sensing riboswitch and the hammerhead ribozyme, and suggests the potential of the 2',5' linkage to elicit a reaction-intermediate conformation without the need to form metalloenzyme complexes. The hairpin ribozyme structures presented here also suggest how water molecules bound at each of the nonbridging oxygens of G+1 may electrostatically stabilize the transition state in a manner that supplements nucleobase functional groups. Such coordination has not been reported for small ribozymes, but is consistent with the structures of protein enzymes. Overall, this work establishes significant parallels between the RNA and protein enzyme worlds.

Indexed as

Base SequenceBinding SitesCatalysisCrystallography, X-RayModels, BiologicalModels, MolecularMolecular Sequence DataNucleic Acid ConformationPhase TransitionRNA, CatalyticRNA StabilityVanadatesWaterRNA, CatalyticVanadatesWater

Identifiers

PMID17488874
PMCPMC1894929
OpenAlexW2143970011

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.