Evidence map›Paper›PMID 32386575›Full record

ArticleMolecular cell2020

Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.

Yong Zi Tan, Lei Zhang, José Rodrigues, Ruixiang Blake Zheng, Sabrina I Giacometti, Ana L Rosário, Brian Kloss, Venkata P Dandey, Hui Wei, Richard Brunton and 11 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
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  4. How many (distinguishable) classes can we identify in single-particle analysis?Acta crystallographica. Section D, Structural biology · 2025
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  5. Article
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  8. Review
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  12. 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
  13. Article
  14. Article
  15. Article
  16. 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
  17. Article
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  19. Review
  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

21 authors at 7 institutions in 4 countries.

Yong Zi TanDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA; National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA.
Lei ZhangDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
José RodriguesInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157 Oeiras, Portugal.
Ruixiang Blake ZhengDepartment of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada.
Sabrina I GiacomettiDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.
Ana L RosárioInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157 Oeiras, Portugal.
Brian KlossCenter on Membrane Protein Production and Analysis, New York Structural Biology Center, New York, NY 10027, USA.
Venkata P DandeyNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA.
Hui WeiNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA.
Richard BruntonDepartment of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada.
Ashleigh M RaczkowskiSimons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA.
Diogo AthaydeInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157 Oeiras, Portugal.
Maria João CatalãoResearch Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisboa, Portugal.
Madalena PimentelResearch Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisboa, Portugal.
Oliver B ClarkeDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA; Department of Anesthesiology, Columbia University, New York, NY 10032, USA.
Todd L LowaryDepartment of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada; Institute of Biological Chemistry, Academia Sinica, Academia Road, Section 2, #128 Nangang, Taipei 11529, Taiwan.
Margarida ArcherInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157 Oeiras, Portugal.
Michael NiederweisDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Clinton S PotterNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA; Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Bridget CarragherNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA; Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: bcarr@nysbc.org.
Filippo ManciaDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: fm123@cumc.columbia.edu.
Columbia University · USNew York Structural Biology Center · USUniversidade Nova de Lisboa · PTUniversity of Alabama at Birmingham · USUniversity of Alberta · CAUniversity of Lisbon · PTInstitute of Biological Chemistry, Academia Sinica · TW

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Training (303-338)P41GM116799 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI HENDRICKSON, WAYNE A. · 2016 to 2020
$7.1M
Structural basis of integral membrane enzyme functionR35GM132120 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Filippo Mancia · 2019 to 2026
$3.7M
Lipid biosynthesis and modification by integral-membrane enzymesR01GM111980 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MANCIA, FILIPPO · 2015 to 2018
$2.2M
Structural basis of phosphoinositide biosynthesis in Mycobacterium tuberculosisR21AI119672 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MANCIA, FILIPPO · 2015 to 2016
$440k
NCRR NIH HHS P41 RR001209NIAID NIH HHS R21 AI119672NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41 GM116799NIGMS NIH HHS R01 GM111980NIGMS NIH HHS R35 GM132120
6 · The paper itself

Abstract

Mycobacterium tuberculosis causes tuberculosis, a disease that kills over 1 million people each year. Its cell envelope is a common antibiotic target and has a unique structure due, in part, to two lipidated polysaccharides-arabinogalactan and lipoarabinomannan. Arabinofuranosyltransferase D (AftD) is an essential enzyme involved in assembling these glycolipids. We present the 2.9-Å resolution structure of M. abscessus AftD, determined by single-particle cryo-electron microscopy. AftD has a conserved GT-C glycosyltransferase fold and three carbohydrate-binding modules. Glycan array analysis shows that AftD binds complex arabinose glycans. Additionally, AftD is non-covalently complexed with an acyl carrier protein (ACP). 3.4- and 3.5-Å structures of a mutant with impaired ACP binding reveal a conformational change, suggesting that ACP may regulate AftD function. Mutagenesis experiments using a conditional knockout constructed in M. smegmatis confirm the essentiality of the putative active site and the ACP binding for AftD function.

Indexed as

Acyl Carrier ProteinBacterial ProteinsCatalytic DomainCell MembraneCell WallCryoelectron MicroscopyGalactansGlycosyltransferasesLipopolysaccharidesMutationMycobacterium smegmatisPhylogenyProtein ConformationSubstrate SpecificityAcyl Carrier ProteinarabinogalactanBacterial ProteinsGalactansGlycosyltransferaseslipoarabinomannanLipopolysaccharidesacyl carrier proteinarabinofuranoseglycosyltransferaselipoarabinomannanlipomannanmembrane proteinMycobacterium tuberculosisnanodiscsingle-particle cryo-electron microscopy

Identifiers

PMID32386575
PMCPMC7263364
OpenAlexW3021075530

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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.