Evidence map›Paper›PMID 33773110›Full record

ArticleCell chemical biology2021

Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.

Christopher D Dawson, Stephania M Irwin, Lindsey R F Backman, Chip Le, Jennifer X Wang, Vyshnavi Vennelakanti, Zhongyue Yang, Heather J Kulik, Catherine L Drennan, Emily P Balskus

Open access · hybridAbstract read
In one paragraph

Article in Cell chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Nitric Oxide Inhibition of Glycyl Radical Enzymes and Their Activases.Journal of the American Chemical Society · 2025
    Article
  6. Article
  7. Article
  8. An unprecedented function for a tungsten-containing oxidoreductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. 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

10 authors at 5 institutions in 1 country.

Christopher D DawsonDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Stephania M IrwinDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
Lindsey R F BackmanDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Chip LeDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
Jennifer X WangHarvard Center for Mass Spectrometry, Faculty of Arts and Sciences Division of Science, Harvard University, 52 Oxford Street, Cambridge, MA 02138, USA.
Vyshnavi VennelakantiDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Zhongyue YangDepartment of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Heather J KulikDepartment of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: hjkulik@mit.edu.
Catherine L DrennanDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: cdrennan@mit.edu.
Emily P BalskusDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA; Broad Institute, Cambridge, MA 02139, USA. Electronic address: balskus@chemistry.harvard.edu.
Massachusetts Institute of Technology · USHarvard University · USBroad Institute · USHoward Hughes Medical Institute · USIIT@MIT · US

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R35 GM126982NIGMS NIH HHS T32 GM007287NIH HHS S10 OD021527
6 · The paper itself

Abstract

Desulfonation of isethionate by the bacterial glycyl radical enzyme (GRE) isethionate sulfite-lyase (IslA) generates sulfite, a substrate for respiration that in turn produces the disease-associated metabolite hydrogen sulfide. Here, we present a 2.7 Å resolution X-ray structure of wild-type IslA from Bilophila wadsworthia with isethionate bound. In comparison with other GREs, alternate positioning of the active site β strands allows for distinct residue positions to contribute to substrate binding. These structural differences, combined with sequence variations, create a highly tailored active site for the binding of the negatively charged isethionate substrate. Through the kinetic analysis of 14 IslA variants and computational analyses, we probe the mechanism by which radical chemistry is used for C-S bond cleavage. This work further elucidates the structural basis of chemistry within the GRE superfamily and will inform structure-based inhibitor design of IsIA and thus of microbial hydrogen sulfide production.

Indexed as

BilophilaCarbonCrystallography, X-RayLyasesModels, MolecularSulfurCarbonLyasesSulfurBilophila wadsworthiacarbon-sulfur bond cleavageglycyl radical enzymehuman gut microbiomehydrogen sulfideisethionatelyasestructural enzymologysulfate-reducing bacteriasulfite

Identifiers

PMID33773110
PMCPMC8473560
OpenAlexW3144270981

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.