Evidence map›Paper›PMID 26513744›Full record

ArticlePloS one2015

Solution Structural Studies of GTP:Adenosylcobinamide-Phosphateguanylyl Transferase (CobY) from Methanocaldococcus jannaschii.

Kiran K Singarapu, Michele M Otte, Marco Tonelli, William M Westler, Jorge C Escalante-Semerena, John L Markley

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. 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.

Kiran K SingarapuNational Magnetic Resonance Facility at Madison and Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, United States of America; Center for NMR and Structural Chemistry, CSIR-Indian Institute of Chemical Technology, Tarnaka, Hyderabad, Telangana, India.
Michele M OtteDepartment of Microbiology, University of Georgia, Athens, Georgia, United States of America.
Marco TonelliNational Magnetic Resonance Facility at Madison and Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
William M WestlerNational Magnetic Resonance Facility at Madison and Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
Jorge C Escalante-SemerenaDepartment of Microbiology, University of Georgia, Athens, Georgia, United States of America.
John L MarkleyNational Magnetic Resonance Facility at Madison and Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
University of Wisconsin–Madison · USUniversity of Georgia · USIndian Institute of Chemical Technology · IN

Funding

TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Request for a supplement for equipmentR37GM040313 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ESCALANTE, JORGE C · 2010 to 2018
$3.5M
NIGMS NIH HHS P41 GM066326NIGMS NIH HHS P41 GM103399NIGMS NIH HHS R37 GM040313
6 · The paper itself

Abstract

gtpadenosylcobinamide-phosphate (AdoCbi-P) guanylyl transferase (CobY) is an enzyme that transfers the GMP moiety of GTP to AdoCbi yielding AdoCbi-GDP in the late steps of the assembly of Ado-cobamides in archaea. The failure of repeated attempts to crystallize ligand-free (apo) CobY prompted us to explore its 3D structure by solution NMR spectroscopy. As reported here, the solution structure has a mixed α/β fold consisting of seven β-strands and five α-helices, which is very similar to a Rossmann fold. Titration of apo-CobY with GTP resulted in large changes in amide proton chemical shifts that indicated major structural perturbations upon complex formation. However, the CobY:GTP complex as followed by 1H-15N HSQC spectra was found to be unstable over time: GTP hydrolyzed and the protein converted slowly to a species with an NMR spectrum similar to that of apo-CobY. The variant CobYG153D, whose GTP complex was studied by X-ray crystallography, yielded NMR spectra similar to those of wild-type CobY in both its apo- state and in complex with GTP. The CobYG153D:GTP complex was also found to be unstable over time.

Indexed as

Models, MolecularMolecular ConformationGuanosine TriphosphateLigandsMethanocaldococcusMultienzyme ComplexesNuclear Magnetic Resonance, BiomolecularNucleotidyltransferasesPentosyltransferasesProtein BindingQuantitative Structure-Activity RelationshipSolutionsGuanosine TriphosphateLigandsMultienzyme Complexesnicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferaseNucleotidyltransferasesPentosyltransferasesSolutions

Identifiers

PMID26513744
PMCPMC4626045
OpenAlexW2149784198

What OpenQuestion holds

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LicenceCC BY
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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.