Evidence map›Paper›PMID 32363534›Full record

ArticleProtein & cell2020

Cryo-EM snapshots of mycobacterial arabinosyltransferase complex EmbB

Lu Zhang, Yao Zhao, Ruogu Gao, Jun Li, Xiuna Yang, Yan Gao, Wei Zhao, Sudagar S Gurcha, Natacha Veerapen, Sarah M Batt and 9 more

Open access · diamondAbstract read
In one paragraph

Article in Protein & cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Target Identification in Anti-Tuberculosis Drug Discovery.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Structure of the priming arabinosyltransferase AftA required for AG biosynthesis ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Editorial: Host immune evasion byFrontiers in immunology · 2022
    Article
  10. Article
  11. Arabinogalactan enhancesFrontiers in immunology · 2022
    Article
  12. Article
  13. Review
  14. 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

19 authors at 7 institutions in 3 countries.

Lu ZhangState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences and College of Pharmacy, Nankai University, Tianjin, 300353, China.
Yao ZhaoShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Ruogu GaoUniversity of Chinese Academy of Sciences, Beijing, 100101, China.
Jun LiShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Xiuna YangShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Yan GaoLaboratory of Structural Biology, Tsinghua University, Beijing, 100084, China.
Wei ZhaoState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences and College of Pharmacy, Nankai University, Tianjin, 300353, China.
Sudagar S GurchaSchool of Biosciences, Institute of Microbiology and Infection, University of Birmingham, Birmingham, B15 2TT, UK.
Natacha VeerapenSchool of Biosciences, Institute of Microbiology and Infection, University of Birmingham, Birmingham, B15 2TT, UK.
Sarah M BattSchool of Biosciences, Institute of Microbiology and Infection, University of Birmingham, Birmingham, B15 2TT, UK.
Kajelle Kaur BesraSchool of Biosciences, Institute of Microbiology and Infection, University of Birmingham, Birmingham, B15 2TT, UK.
Wenqing XuShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Lijun BiNational Laboratory of Biomacromolecules and Key Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing, 100101, China.
Xian'en ZhangNational Laboratory of Biomacromolecules and Key Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing, 100101, China.
Luke W GuddatSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, 4072, Australia.
Haitao YangShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Quan WangShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China. wangq@ibp.ac.cn.
Gurdyal S BesraSchool of Biosciences, Institute of Microbiology and Infection, University of Birmingham, Birmingham, B15 2TT, UK. G.Besra@bham.ac.uk.
Zihe RaoState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences and College of Pharmacy, Nankai University, Tianjin, 300353, China. raozh@tsinghua.edu.cn.
ShanghaiTech University · CNUniversity of Birmingham · GBInstitute of Biophysics · CNNankai University · CNChinese Academy of Sciences · CNTsinghua University · CNUniversity of Queensland · AU

Funding

Medical Research Council MR/S000542/1
6 · The paper itself

Abstract

Inhibition of Mycobacterium tuberculosis (Mtb) cell wall assembly is an established strategy for anti-TB chemotherapy. Arabinosyltransferase EmbB, which catalyzes the transfer of arabinose from the donor decaprenyl-phosphate-arabinose (DPA) to its arabinosyl acceptor is an essential enzyme for Mtb cell wall synthesis. Analysis of drug resistance mutations suggests that EmbB is the main target of the front-line anti-TB drug, ethambutol. Herein, we report the cryo-EM structures of Mycobacterium smegmatis EmbB in its "resting state" and DPA-bound "active state". EmbB is a fifteen-transmembrane-spanning protein, assembled as a dimer. Each protomer has an associated acyl-carrier-protein (AcpM) on their cytoplasmic surface. Conformational changes upon DPA binding indicate an asymmetric movement within the EmbB dimer during catalysis. Functional studies have identified critical residues in substrate recognition and catalysis, and demonstrated that ethambutol inhibits transferase activity of EmbB by competing with DPA. The structures represent the first step directed towards a rational approach for anti-TB drug discovery.

Indexed as

Cryoelectron MicroscopyBacterial ProteinsEthambutolMycobacterium smegmatisPentosyltransferasesarabinosyltransferaseBacterial ProteinsEthambutolPentosyltransferasesacyl-carrier-proteinarabinoglacatanarabinosyltransferasecell wall synthesiscryo-EMdrug discoveryEmbBethambutolMycobacterium tuberculosis

Identifiers

PMID32363534
PMCPMC7305291
OpenAlexW3022127239

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.