Evidence map›Paper›PMID 34295570›Full record

ArticleACS catalysis2020

Editing Domain Motions Preorganize the Synthetic Active Site of Prolyl-tRNA Synthetase.

Quin H Hu, Murphi T Williams, Irina Shulgina, Carl J Fossum, Katelyn M Weeks, Lauren M Adams, Clorice R Reinhardt, Karin Musier-Forsyth, Sanchita Hati, Sudeep Bhattacharyya

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

Article in ACS catalysis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
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  4. 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

10 authors at 2 institutions in 1 country.

Quin H HuDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.
Murphi T WilliamsDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.
Irina ShulginaDepartment of Chemistry and Biochemistry and Center for RNA Biology, The Ohio State University, Columbus, OH, 43210, USA.
Carl J FossumDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.
Katelyn M WeeksDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.
Lauren M AdamsDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.
Clorice R ReinhardtDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.
Karin Musier-ForsythDepartment of Chemistry and Biochemistry and Center for RNA Biology, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0002-0354-4172
Sanchita HatiDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.ORCID 0000-0002-7452-0872
Sudeep BhattacharyyaDepartment of Chemistry and Biochemistry, University of Wisconsin-Eau Claire, WI, 54701, USA.ORCID 0000-0002-3960-1239
University of Wisconsin–Eau Claire · USThe Ohio State University · US

Funding

Translational quality control by trans-editing domainsR01GM113656 · NIGMS · OHIO STATE UNIVERSITY · PI MUSIER-FORSYTH, KARIN M · 2015 to 2018
$1.1M
Exploring the Dynamics of Prolyl-tRNA Synthetases: Towards Developing a Screening Method for Species-Specific InhibitorsR15GM117510 · NIGMS · UNIVERSITY OF WISCONSIN EAU CLAIRE · PI BHATTACHARYAY, SUDEEP, HATI, SANCHITA · 2016 to 2023
$878k
NIGMS NIH HHS R01 GM113656NIGMS NIH HHS R15 GM117510
6 · The paper itself

Abstract

Prolyl-tRNA synthetases (ProRSs) catalyze the covalent attachment of proline onto cognate tRNAs, an indispensable step for protein synthesis in all living organisms. ProRSs are modular enzymes and the "prokaryotic-like" ProRSs are distinguished from "eukaryotic-like" ProRSs by the presence of an editing domain (INS) inserted between motifs 2 and 3 of the main catalytic domain. Earlier studies suggested the presence of coupled-domain dynamics could contribute to catalysis; however, the role that the distal, highly mobile INS domain plays in catalysis at the synthetic active site is not completely understood. In the present study, a combination of theoretical and experimental approaches has been used to elucidate the precise role of INS domain dynamics. Quantum mechanical/molecular mechanical simulations were carried out to model catalytic Pro-AMP formation by

Indexed as

Aminoacyl tRNA synthetasecoupled-domain motionsenzyme catalysis simulationspreorganizationprotein dynamicsquantum mechanical/molecular mechanical simulationsreorganization

Identifiers

PMID34295570
PMCPMC8293909
OpenAlexW3049173260

What OpenQuestion holds

Textmetadata
LicenceTDM
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.