Evidence map›Paper›PMID 23851074›Full record

ArticleFEBS letters2013

Crystal structure of the ligand-binding form of nanoRNase from Bacteroides fragilis, a member of the DHH/DHHA1 phosphoesterase family of proteins.

Yuri Uemura, Noriko Nakagawa, Taisuke Wakamatsu, Kwang Kim, Gaetano Thomas Montelione, John Francis Hunt, Seiki Kuramitsu, Ryoji Masui

Abstract read
In one paragraph

Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
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  6. Review
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  8. 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

8 authors.

Yuri UemuraGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.
Noriko Nakagawa
Taisuke Wakamatsu
Kwang Kim
Gaetano Thomas Montelione
John Francis Hunt
Seiki Kuramitsu
Ryoji Masui

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI GOUAUX, JAMES E · 2005 to 2009
$16.8M
NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

NanoRNase (Nrn) specifically degrades nucleoside 3',5'-bisphosphate and the very short RNA, nanoRNA, during the final step of mRNA degradation. The crystal structure of Nrn in complex with a reaction product GMP was determined. The overall structure consists of two domains that are interconnected by a flexible loop and form a cleft. Two Mn²⁺ ions are coordinated by conserved residues in the DHH motif of the N-terminal domain. GMP binds near the DHHA1 motif region in the C-terminal domain. Our structure enables us to predict the substrate-bound form of Nrn as well as other DHH/DHHA1 phosphoesterase family proteins.

Indexed as

Amino Acid MotifsBacterial ProteinsBacteroidesBinding SitesCrystallography, X-RayEscherichia coliLigandsManganeseModels, MolecularProtein BindingProtein ConformationRibonucleasesRNARNA, MessengerSubstrate SpecificityBacterial ProteinsLigandsManganesenanoRNase, Bacteroides fragilisRibonucleasesRNARNA, Messengeradenosine 3′,5′-bisphosphatebfNrnCrystal structureDHH/DHHA1 familyguanosine 3′,5′-bisphosphatemRNA degradationnanoRNAnanoRNasenanoRNase of Bacteroides fragilisnanoRNase of Staphylococcus haemolyticusnanoRNase of Thermus thermophilus HB8NrnpAppGpRecJ exonuclease of T. thermophilus HB8shNrnttNrnttRecJ

Identifiers

PMID23851074
PMCPMC4113422

What OpenQuestion holds

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Registered trials

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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.