Evidence map›Paper›PMID 18073106›Full record

ArticleStructure (London, England : 1993)2007

Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes.

Dario Segura-Peña, Joseph Lichter, Manuela Trani, Manfred Konrad, Arnon Lavie, Stefan Lutz

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2007. 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
0.9field-weighted citation impact, top 26% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Cyclic oligomer design with de novo αβ-proteins.Protein science : a publication of the Protein Society · 2017
    Article
  4. Article
  5. Article
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  8. Article
  9. Review
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  13. Deprotonated imidodiphosphate in AMPPNP-containing protein structures.Acta crystallographica. Section D, Biological crystallography · 2011
    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

6 authors at 3 institutions in 2 countries.

Dario Segura-PeñaDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 South Ashland Avenue, Chicago, IL 60607, USA.
Joseph Lichter
Manuela Trani
Manfred Konrad
Arnon Lavie
Stefan Lutz
Emory University · USUniversity of Illinois Chicago · USMax Planck Society · DE

Funding

Virology and Molecular Biomarkers CoreP30AI050409 · NIAID · EMORY UNIVERSITY · PI Carlos del Rio · 2002 to 2026
$74.0M
STRUCTURAL BIOLOGY OF ENZYMES ACTIVATING PRODRUGSR01AI046943 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LAVIE, ARNON · 2001 to 2008
$1.7M
Improving nucleoside phosphorylation with hybrid kinasesR01GM069958 · NIGMS · EMORY UNIVERSITY · PI LUTZ, STEFAN · 2005 to 2009
$1.2M
NIAID NIH HHS AI046943NIAID NIH HHS AI050409NIAID NIH HHS P30 AI050409NIAID NIH HHS R01 AI046943NIGMS NIH HHS GM69958NIGMS NIH HHS R01 GM069958
6 · The paper itself

Abstract

The human cytosolic thymidine kinase (TK) and structurally related TKs in prokaryotes play a crucial role in the synthesis and regulation of the cellular thymidine triphosphate pool. We report the crystal structures of the TK homotetramer from Thermotoga maritima in four different states: its apo-form, a binary complex with thymidine, as well as the ternary structures with the two substrates (thymidine/AppNHp) and the reaction products (TMP/ADP). In combination with fluorescence spectroscopy and mutagenesis experiments, our results demonstrate that ATP binding is linked to a substantial reorganization of the enzyme quaternary structure, leading to a transition from a closed, inactive conformation to an open, catalytic state. We hypothesize that these structural changes are relevant to enzyme function in situ as part of the catalytic cycle and serve an important role in regulating enzyme activity by amplifying the effects of feedback inhibitor binding.

Indexed as

Adenosine TriphosphateDisulfidesKineticsModels, MolecularMutagenesis, Site-DirectedProtein BindingProtein Structure, QuaternarySpectrometry, FluorescenceThymidine KinaseX-Ray DiffractionAdenosine TriphosphateDisulfidesThymidine Kinasethymidine kinase 1

Identifiers

PMID18073106
PMCPMC2180243
OpenAlexW2071744343

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.