Evidence map›Paper›PMID 23487447›Full record

ArticleJournal of virology2013

Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: implication for a trans mechanism of VPg uridylylation.

Cheng Chen, Yaxin Wang, Chao Shan, Yuna Sun, Peng Xu, Honggang Zhou, Cheng Yang, Pei-Yong Shi, Zihe Rao, Bo Zhang and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 82 citations in OpenAlex.

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  14. Functional advantages of triplication of the 3B coding region of the FMDV genome.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
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  20. Enterovirus A71 Proteins: Structure and Function.Frontiers in microbiology · 2018
    Review
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

11 authors at 6 institutions in 2 countries.

Cheng ChenStructural Biology Laboratory and MOE Laboratory of Protein Science, School of Medicine and Life Science, Tsinghua University, Beijing, China.
Yaxin Wang
Chao Shan
Yuna Sun
Peng Xu
Honggang Zhou
Cheng Yang
Pei-Yong Shi
Zihe Rao
Bo Zhang
Zhiyong Lou
Tsinghua University · CNInstitute of Biophysics · CNWuhan Institute of Virology · CNNankai University · CNTianjin International Joint Academy of Biomedicine · CNWadsworth Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Picornavirus RNA replication is initiated by VPg uridylylation, during which the hydroxyl group of the third tyrosine residue of the virally encoded protein VPg is covalently linked to two UMP molecules by RNA-dependent RNA polymerase (RdRp; also known as 3D(pol)). We previously identified site 311, located at the base of the palm domain of the enterovirus 71 (EV71) RdRp, to be the site for EV71 VPg binding and uridylylation. Here we report the crystal structure of EV71 3D(pol) complexed with VPg. VPg was anchored at the bottom of the palm domain of the 3D(pol) molecule and exhibited an extended V-shape conformation. The corresponding interface on 3D(pol) was mainly formed by residues within site 311 and other residues in the palm and finger domains. Mutations of the amino acids of 3D(pol) involved in the VPg interaction (3DL319A, 3DD320A, and 3DY335A) significantly disrupted VPg binding to 3D(pol), resulting in defective VPg uridylylation. In contrast, these mutations did not affect the RNA elongation activity of 3D(pol). In the context of viral genomic RNA, mutations that abolished VPg uridylylation activity were lethal for EV71 replication. Further in vitro analysis showed that the uridylylation activity was restored by mixing VPg-binding-defective and catalysis-defective mutants, indicating a trans mechanism for EV71 VPg uridylylation. Our results, together with previous results of other studies, demonstrate that different picornaviruses use distinct binding sites for VPg uridylylation.

Indexed as

AnimalsChlorocebus aethiopsCrystallography, X-RayEnterovirus A, HumanMutagenesis, Site-DirectedMutant ProteinsProtein BindingProtein Structure, QuaternaryRNA-Dependent RNA PolymeraseTyrosineUridine MonophosphateVero CellsViral ProteinsMutant ProteinsRNA-Dependent RNA PolymeraseTyrosineUridine MonophosphateViral Proteins

Identifiers

PMID23487447
PMCPMC3648134
OpenAlexW2111302701

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.