Evidence map›Paper›PMID 21667997›Full record

ArticleJournal of the American Chemical Society2011

Hydrogen-bonding capability of a templating difluorotoluene nucleotide residue in an RB69 DNA polymerase ternary complex.

Shuangluo Xia, William H Konigsberg, Jimin Wang

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
  2. Review
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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.

Shuangluo XiaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
William H Konigsberg
Jimin Wang

Funding

Molecular Biology and Structure of a DNA ReplicaseR01GM063276 · NIGMS · YALE UNIVERSITY · PI KONIGSBERG, WILLIAM H · 2001 to 2013
$4.2M
NIGMS NIH HHS R01 GM063276NIGMS NIH HHS R01-GM063276-09
6 · The paper itself

Abstract

Results obtained using 2,4-difluorotoluene nucleobase (dF) as a nonpolar thymine isostere by Kool and colleagues challenged the Watson-Crick dogma that hydrogen bonds between complementary bases are an absolute requirement for accurate DNA replication. Here, we report crystal structure of an RB69 DNA polymerase L561A/S565G/Y567A triple mutant ternary complex with a templating dF opposite dTTP at 1.8 Å-resolution. In this structure, direct hydrogen bonds were observed between: (i) dF and the incoming dTTP, (ii) dF and residue G568 of the polymerase, and (iii) dF and ordered water molecules surrounding the nascent base pair. Therefore, this structure provides evidence that a templating dF can form novel hydrogen bonds with the incoming dTTP and with the enzyme that differ from those formed with a templating dT.

Indexed as

Crystallography, X-RayDNA-Directed DNA PolymeraseHydrogen BondingModels, MolecularMutationProtein Structure, TertiaryThymine NucleotidesTolueneViral Proteinsbacteriophage RB69 DNA polymerasedifluorotolueneDNA-Directed DNA Polymerasethymidine 5'-triphosphateThymine NucleotidesTolueneViral Proteins

Identifiers

PMID21667997
PMCPMC3139434

What OpenQuestion holds

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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.