Evidence map›Paper›PMID 33707784›Full record

ArticleNature chemical biology2021

Functional elucidation of TfuA in peptide backbone thioamidation.

Andi Liu, Yuanyuan Si, Shi-Hui Dong, Nilkamal Mahanta, Haley N Penkala, Satish K Nair, Douglas A Mitchell

Abstract read
In one paragraph

Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

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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

20 citing papers in PubMed.

  1. Article
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  16. Article
  17. Article
  18. A Cobalamin-Dependent Radical SAM Enzyme Catalyzes the Unique CAngewandte Chemie (International ed. in English) · 2022
    Article
  19. 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

7 authors.

Andi LiuDepartment of Microbiology, University of Illinois, Urbana, IL, USA.
Yuanyuan SiCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, IL, USA.
Shi-Hui DongDepartment of Biochemistry, University of Illinois, Urbana, IL, USA.ORCID http://orcid.org/0000-0002-1743-2163
Nilkamal MahantaCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, IL, USA.
Haley N PenkalaDepartment of Microbiology, University of Illinois, Urbana, IL, USA.
Satish K NairCarl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, IL, USA.
Douglas A MitchellDepartment of Microbiology, University of Illinois, Urbana, IL, USA. douglasm@illinois.edu.ORCID http://orcid.org/0000-0002-9564-0953

Funding

Enzyme Chemistry and Biological Function of RiPP-like Modifications.R01GM097142 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2012 to 2024
$4.1M
Structural Biological Studies of Thipeptide Biosynthesis and EngineeringR01GM131347 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI NAIR, SATISH K · 2019 to 2022
$1.2M
4800 Plus MALDI TOF/TOF AnalyzerS10RR027109 · NCRR · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2010 to 2010
$395k
NCRR NIH HHS S10 RR027109NIGMS NIH HHS R01 GM097142NIGMS NIH HHS R01 GM131347
6 · The paper itself

Abstract

YcaO enzymes catalyze several post-translational modifications on peptide substrates, including thioamidation, which substitutes an amide oxygen with sulfur. Most predicted thioamide-forming YcaO enzymes are encoded adjacent to TfuA, which when present, is required for thioamidation. While activation of the peptide amide backbone is well established for YcaO enzymes, the function of TfuA has remained enigmatic. Here we characterize the TfuA protein involved in methyl-coenzyme M reductase thioamidation and demonstrate that TfuA catalyzes the hydrolysis of thiocarboxylated ThiS (ThiS-COSH), a proteinaceous sulfur donor, and enhances the affinity of YcaO toward the thioamidation substrate. We also report a crystal structure of a TfuA, which displays a new protein fold. Our structural and mutational analyses of TfuA have uncovered conserved binding interfaces with YcaO and ThiS in addition to revealing a hydrolase-like active site featuring a Ser-Lys catalytic pair.

Indexed as

Archaeal ProteinsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliEuryarchaeotaGene ExpressionGenetic VectorsHistidineKineticsMannose-Binding LectinMethanobacteriaceaeMethanocaldococcusModels, MolecularMutationOligopeptidesArchaeal ProteinsHis-His-His-His-His-HisHistidineMannose-Binding Lectinmethyl coenzyme M reductaseOligopeptidesOxidoreductasesPeptidesRecombinant Fusion ProteinsThioamides

Identifiers

PMID33707784
PMCPMC8084935

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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.