Evidence map›Paper›PMID 17407781›Full record

ArticleJournal of molecular biology2007

Binding of ATP to TK1-like enzymes is associated with a conformational change in the quaternary structure.

Dario Segura-Peña, Stefan Lutz, Christian Monnerjahn, Manfred Konrad, Arnon Lavie

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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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

5 authors at 4 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.
Stefan Lutz
Christian Monnerjahn
Manfred Konrad
Arnon Lavie
Ashland (United States) · USEmory University · USMax Planck Institute for Biophysical Chemistry · DEMax Planck Society · DE

Funding

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 R01 AI046943NIGMS NIH HHS R01 GM069958
6 · The paper itself

Abstract

Human thymidine kinase 1 (hTK1) and structurally related TKs from other organisms catalyze the initial phosphorylation step in the thymidine salvage pathway. Though ATP is known to be the preferred phosphoryl donor for TK1-like enzymes, its exact binding mode and effect on the oligomeric state has not been analyzed. Here we report the structures of hTK1 and of the Thermotoga maritima thymidine kinase (TmTK) in complex with the bisubstrate inhibitor TP4A. The TmTK-TP4A structure reveals that the adenosine moiety of ATP binds at the subunit interface of the homotetrameric enzyme and that the majority of the ATP-enzyme interactions occur between the phosphate groups and the P-loop. In the hTK1 structure the adenosine group of TP4A exhibited no electron density. This difference between hTK1 and TmTK is rationalized by a difference in the conformation of their quaternary structure. A more open conformation, as seen in the TmTK-TP4A complex structure, is required to provide space for the adenosine moiety. Our analysis supports the formation of an analogous open conformation in hTK1 upon ATP binding.

Indexed as

Adenosine TriphosphateAmino Acid SequenceBinding SitesCrystallography, X-RayDimerizationHumansKineticsMolecular Sequence DataProtein BindingProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondaryStructure-Activity RelationshipThermotoga maritimaThymidineThymidine KinaseAdenosine TriphosphateThymidineThymidine Kinasethymidine kinase 1

Identifiers

PMID17407781
PMCPMC1899836
OpenAlexW1966661437

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.