Evidence map›Paper›PMID 27428510›Full record

ArticleNature chemical biology2016

Structure and function of the bacterial decapping enzyme NudC.

Katharina Höfer, Sisi Li, Florian Abele, Jens Frindert, Jasmin Schlotthauer, Julia Grawenhoff, Jiamu Du, Dinshaw J Patel, Andres Jäschke

Abstract read
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 86 citations in OpenAlex.

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  15. RNA (New York, N.Y.) · 2022
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  16. Non-coding RNA · 2022
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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

9 authors at 3 institutions in 3 countries.

Katharina HöferInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Sisi LiStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA.
Florian AbeleInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Jens FrindertInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Jasmin SchlotthauerInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Julia GrawenhoffInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Jiamu DuShanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-1337-0786
Dinshaw J PatelStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA.
Andres JäschkeInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Heidelberg University · DEMemorial Sloan Kettering Cancer Center · USChinese Academy of Sciences · CN

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Posttranscriptional regulation by mRNA-binding shuttling and transport proteinsR01GM104962 · NIGMS · ROCKEFELLER UNIVERSITY · PI OHLER, UWE, PATEL, DINSHAW J · 2012 to 2016
$4.4M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM104962
6 · The paper itself

Abstract

RNA capping and decapping are thought to be distinctive features of eukaryotes. The redox cofactor NAD was recently discovered to be attached to small regulatory RNAs in bacteria in a cap-like manner, and Nudix hydrolase NudC was found to act as a NAD-decapping enzyme in vitro and in vivo. Here, crystal structures of Escherichia coli NudC in complex with substrate NAD and with cleavage product NMN reveal the catalytic residues lining the binding pocket and principles underlying molecular recognition of substrate and product. Biochemical mutation analysis identifies the conserved Nudix motif as the catalytic center of the enzyme, which needs to be homodimeric, as the catalytic pocket is composed of amino acids from both monomers. NudC is single-strand specific and has a purine preference for the 5'-terminal nucleotide. The enzyme strongly prefers NAD-linked RNA (NAD-RNA) over NAD and binds to a diverse set of cellular RNAs in an unspecific manner.

Indexed as

BiocatalysisCrystallography, X-RayEscherichia coliModels, MolecularNudix HydrolasesProtein ConformationPyrophosphatasesNudix HydrolasesPyrophosphatases

Identifiers

PMID27428510
PMCPMC5003112
OpenAlexW2487738497

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.