Evidence map›Paper›PMID 23161756›Full record

ArticleProteins2013

A broad specificity nucleoside kinase from Thermoplasma acidophilum.

Sarah R Elkin, Abhinav Kumar, Carol W Price, Linda Columbus

Abstract read
In one paragraph

Article in Proteins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Objective: biochemical function.Frontiers in genetics · 2014
    Article
  6. Article
  7. Known structure, unknown function: An inquiry-based undergraduate biochemistry laboratory course.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology
    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

4 authors.

Sarah R ElkinDepartment of Chemistry, University of Virginia, Charlottesville, VA 22904-4319, USA.
Abhinav Kumar
Carol W Price
Linda Columbus

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2005 to 2009
$50.6M
Structure Determination Core at SSRLU54GM094586 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI LESLEY, SCOTT ALLAN · 2010 to 2014
$40.1M
SciBay: A New Methodology for Scientific Collaboration and Gene Function DetermiRC2GM092602 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI KASIF, SIMON, ROBERTS, RICHARD J · 2009 to 2010
$4.0M
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS RC2 GM092602NIGMS NIH HHS RC2-GM-092602NIGMS NIH HHS U54 GM074898NIGMS NIH HHS U54 GM094586NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The crystal structure of Ta0880, determined at 1.91 Å resolution, from Thermoplasma acidophilum revealed a dimer with each monomer composed of an α/β/α sandwich domain and a smaller lid domain. The overall fold belongs to the PfkB family of carbohydrate kinases (a family member of the Ribokinase clan) which include ribokinases, 1-phosphofructokinases, 6-phosphofructo-2-kinase, inosine/guanosine kinases, fructokinases, adenosine kinases, and many more. Based on its general fold, Ta0880 had been annotated as a ribokinase-like protein. Using a coupled pyruvate kinase/lactate dehydrogenase assay, the activity of Ta0880 was assessed against a variety of ribokinase/pfkB-like family substrates; activity was not observed for ribose, fructose-1-phosphate, or fructose-6-phosphate. Based on structural similarity with nucleoside kinases (NK) from Methanocaldococcus jannaschii (MjNK, PDB 2C49, and 2C4E) and Burkholderia thailandensis (BtNK, PDB 3B1O), nucleoside kinase activity was investigated. Ta0880 (TaNK) was confirmed to have nucleoside kinase activity with an apparent KM for guanosine of 0.21 μM and catalytic efficiency of 345,000 M(-1) s(-1) . These three NKs have significantly different substrate, phosphate donor, and cation specificities and comparisons of specificity and structure identified residues likely responsible for the nucleoside substrate selectivity. Phylogenetic analysis identified three clusters within the PfkB family and indicates that TaNK is a member of a new sub-family with broad nucleoside specificities. Proteins 2013. © 2012 Wiley Periodicals, Inc.

Indexed as

Amino Acid SequenceBurkholderiaCrystallography, X-RayKineticsMethanococcalesMolecular Sequence DataPhosphotransferasesProtein MultimerizationProtein Structure, SecondarySequence AlignmentSubstrate SpecificityThermoplasmanucleoside phosphotransferasePhosphotransferases

Identifiers

PMID23161756
PMCPMC3595323

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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.