Evidence map›Paper›PMID 27380375›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Crystallographic analysis of a subcomplex of the transsulfursome with tRNA for Cys-tRNA(Cys) synthesis.

Meirong Chen, Yuto Nakazawa, Yume Kubo, Nozomi Asano, Koji Kato, Isao Tanaka, Min Yao

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 31% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Meirong ChenGraduate School of Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Yuto NakazawaGraduate School of Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Yume KuboGraduate School of Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Nozomi AsanoGraduate School of Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Koji KatoGraduate School of Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Isao TanakaFaculty of Advanced Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Min YaoGraduate School of Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In most organisms, Cys-tRNA(Cys) is directly synthesized by cysteinyl-tRNA synthetase (CysRS). Many methanogenic archaea, however, use a two-step, indirect pathway to synthesize Cys-tRNA(Cys) owing to a lack of CysRS and cysteine-biosynthesis systems. This reaction is catalyzed by O-phosphoseryl-tRNA synthetase (SepRS), Sep-tRNA:Cys-tRNA synthase (SepCysS) and SepRS/SepCysS pathway enhancer (SepCysE) as the transsulfursome, in which SepCysE connects both SepRS and SepCysS. On the transsulfursome, SepRS first ligates an O-phosphoserine to tRNA(Cys), and the mischarged intermediate Sep-tRNA(Cys) is then transferred to SepCysS, where it is further modified to Cys-tRNA(Cys). In this study, a subcomplex of the transsulfursome with tRNA(Cys) (SepCysS-SepCysE-tRNA(Cys)), which is involved in the second reaction step of the indirect pathway, was constructed and then crystallized. The crystals diffracted X-rays to a resolution of 2.6 Å and belonged to space group P6522, with unit-cell parameters a = b = 107.2, c = 551.1 Å. The structure determined by molecular replacement showed that the complex consists of a SepCysS dimer, a SepCysE dimer and one tRNA(Cys) in the asymmetric unit.

Indexed as

Amino Acid SequenceAmino Acyl-tRNA SynthetasesArchaeal ProteinsCloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliGene ExpressionMethanocaldococcusPlasmidsRecombinant ProteinsRNA, Transfer, CysX-Ray DiffractionAmino Acyl-tRNA SynthetasesArchaeal Proteinscysteinyl-tRNA synthetaseRecombinant ProteinsRNA, Transfer, CysCys-tRNACysSepCysESepCysSSepRStranssulfursome

Identifiers

PMID27380375
PMCPMC4933008
OpenAlexW2471100755

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.