Evidence map›Paper›PMID 28893989›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Structures of the peptide-modifying radical SAM enzyme SuiB elucidate the basis of substrate recognition.

Katherine M Davis, Kelsey R Schramma, William A Hansen, John P Bacik, Sagar D Khare, Mohammad R Seyedsayamdost, Nozomi Ando

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 104 citations in OpenAlex.

  1. Mechanistic insight into radicalNatural product reports · 2026
    Review
  2. Myxarylin: TotalJournal of the American Chemical Society · 2026
    Article
  3. RadicalJournal of the American Chemical Society · 2026
    Article
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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 at 2 institutions in 1 country.

Katherine M DavisDepartment of Chemistry, Princeton University, Princeton, NJ 08544.
Kelsey R SchrammaDepartment of Chemistry, Princeton University, Princeton, NJ 08544.
William A HansenDepartment of Chemistry and Chemical Biology, Rutgers University, New Brunswick, NJ 08901.
John P BacikDepartment of Chemistry, Princeton University, Princeton, NJ 08544.
Sagar D KhareDepartment of Chemistry and Chemical Biology, Rutgers University, New Brunswick, NJ 08901.ORCID 0000-0002-2255-0543
Mohammad R SeyedsayamdostDepartment of Chemistry, Princeton University, Princeton, NJ 08544; mrseyed@princeton.edu nozomi.ando@princeton.edu.
Nozomi AndoDepartment of Chemistry, Princeton University, Princeton, NJ 08544; mrseyed@princeton.edu nozomi.ando@princeton.edu.
Princeton University · USRutgers, The State University of New Jersey · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Structural Characterizations of Transient and Heterogeneous Protein ComplexesR00GM100008 · NIGMS · PRINCETON UNIVERSITY · PI ANDO, NOZOMI · 2014 to 2016
$747k
Molecular Analysis of Metabolites and Signaling Networks in Microbial SymbiosesR00GM098299 · NIGMS · PRINCETON UNIVERSITY · PI SEYEDSAYAMDOST, MOHAMMAD R · 2013 to 2015
$747k
Structural Characterizations of Transient and Heterogeneous Protein ComplexesK99GM100008 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ANDO, NOZOMI · 2012 to 2013
$176k
Molecular Analysis of Metabolites and Signaling Networks in Microbial SymbiosesK99GM098299 · NIGMS · HARVARD MEDICAL SCHOOL · PI SEYEDSAYAMDOST, MOHAMMAD R · 2011 to 2012
$135k
NIGMS NIH HHS K99 GM098299NIGMS NIH HHS K99 GM100008NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R00 GM098299NIGMS NIH HHS R00 GM100008
6 · The paper itself

Abstract

Posttranslational modification of ribosomally synthesized peptides provides an elegant means for the production of biologically active molecules known as RiPPs (ribosomally synthesized and posttranslationally modified peptides). Although the leader sequence of the precursor peptide is often required for turnover, the exact mode of recognition by the modifying enzymes remains unclear for many members of this class of natural products. Here, we have used X-ray crystallography and computational modeling to examine the role of the leader peptide in the biosynthesis of a homolog of streptide, a recently identified peptide natural product with an intramolecular lysine-tryptophan cross-link, which is installed by the radical

Indexed as

Computational BiologyCrystallography, X-RayModels, MolecularPhosphotransferases (Alcohol Group Acceptor)Protein BindingProtein BiosynthesisProtein Processing, Post-TranslationalProtein Sorting SignalsProtein Structure, SecondaryS-AdenosylmethionineStreptococcusPhosphotransferases (Alcohol Group Acceptor)Protein Sorting SignalsS-Adenosylmethioninestreptomycin 3''-kinaseradical SAM enzymeRiPPRRE domainSPASM domainstreptide

Identifiers

PMID28893989
PMCPMC5625900
OpenAlexW2753698499

What OpenQuestion holds

Textmetadata
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.