Evidence map›Paper›PMID 23192021›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012

ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.

T Petrova, E Y Bezsudnova, K M Boyko, A V Mardanov, K M Polyakov, V V Volkov, M Kozin, N V Ravin, I G Shabalin, K G Skryabin and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Temperature adaptation of DNA ligases from psychrophilic organisms.Extremophiles : life under extreme conditions · 2019
    Article
  6. Article
  7. Article
  8. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. 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

13 authors at 5 institutions in 1 country.

T PetrovaBach Institute of Biochemistry, RAS, Leninsky pr. 33, Moscow 119071, Russian Federation. petrova@impb.psn.ru
E Y Bezsudnova
K M Boyko
A V Mardanov
K M Polyakov
V V Volkov
M Kozin
N V Ravin
I G Shabalin
K G Skryabin
T N Stekhanova
M V Kovalchuk
V O Popov
A N Bach Institute of Biochemistry · RUA.V. Shubnikov Institute of Crystallography · RUKurchatov Institute · RUBioengineering Center · RUInstitute of Mathematical Problems of Biology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been revealed: closed and open extended conformations. The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 (LigTh1519) in the crystalline state determined at a resolution of 3.02 Å shows a new relative arrangement of the OB-fold domain which is intermediate between the positions of this domain in the closed and the open extended conformations of previously determined archaeal DNA ligases. However, small-angle X-ray scattering (SAXS) measurements indicate that in solution the LigTh1519 molecule adopts either an open extended conformation or both an intermediate and an open extended conformation with the open extended conformation being dominant.

Indexed as

Adenosine TriphosphateArchaeal ProteinsBinding SitesCrystallography, X-RayDNA, ArchaealDNA Breaks, Single-StrandedDNA Ligase ATPDNA LigasesModels, MolecularProtein FoldingScattering, Small AngleThermococcusAdenosine TriphosphateArchaeal ProteinsDNA, ArchaealDNA Ligase ATPDNA Ligases

Identifiers

PMID23192021
PMCPMC3509962
OpenAlexW2062511701

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.