Evidence map›Paper›PMID 32923628›Full record

ArticleScience advances2020

Crystal structure of a YeeE/YedE family protein engaged in thiosulfate uptake.

Yoshiki Tanaka, Kunihito Yoshikaie, Azusa Takeuchi, Muneyoshi Ichikawa, Tomoyuki Mori, Sayaka Uchino, Yasunori Sugano, Toshio Hakoshima, Hiroshi Takagi, Gen Nonaka and 1 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  6. Identification of theMicrobiology (Reading, England) · 2025
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  14. Infection and immunity · 2024
    Article
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  18. Review
  19. In the AlphaproteobacteriumAntioxidants (Basel, Switzerland) · 2023
    Article
  20. 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

11 authors at 3 institutions in 3 countries.

Yoshiki TanakaNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.ORCID 0000-0001-6960-5276
Kunihito YoshikaieNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Azusa TakeuchiNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Muneyoshi IchikawaNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.ORCID 0000-0002-5921-7699
Tomoyuki MoriNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.ORCID 0000-0003-2019-5370
Sayaka UchinoNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.ORCID 0000-0001-9206-3831
Yasunori SuganoNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Toshio HakoshimaNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Hiroshi TakagiNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.ORCID 0000-0002-1786-3174
Gen NonakaAjinomoto-Genetika Research Institute, Moscow 117545, Russia.ORCID 0000-0003-3362-8067
Tomoya TsukazakiNara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.ORCID 0000-0002-6386-723X
Nara Institute of Science and Technology · JPAjinomoto (United States) · USThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have demonstrated that a bacterial membrane protein, YeeE, mediates thiosulfate uptake. Thiosulfate is used for cysteine synthesis in bacteria as an inorganic sulfur source in the global biological sulfur cycle. The crystal structure of YeeE at 2.5-Å resolution reveals an unprecedented hourglass-like architecture with thiosulfate in the positively charged outer concave side. YeeE is composed of loops and 13 helices including 9 transmembrane α helices, most of which show an intramolecular pseudo 222 symmetry. Four characteristic loops are buried toward the center of YeeE and form its central region surrounded by the nine helices. Additional electron density maps and successive molecular dynamics simulations imply that thiosulfate can remain temporally at several positions in the proposed pathway. We propose a plausible mechanism of thiosulfate uptake via three important conserved cysteine residues of the loops along the pathway.

Identifiers

PMID32923628
PMCPMC7449682
OpenAlexW3080597954

What OpenQuestion holds

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LicenceCC BY-NC
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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.