Evidence map›Paper›PMID 31366889›Full record

ArticleNature communications2019

The structural basis of N-acyl-α-amino-β-lactone formation catalyzed by a nonribosomal peptide synthetase.

Dale F Kreitler, Erin M Gemmell, Jason E Schaffer, Timothy A Wencewicz, Andrew M Gulick

Open access · greenAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

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

34 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  5. Review
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  13. Determining Protein Structures Using X-Ray Crystallography.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. β-Lactams from the Ocean.Marine drugs · 2023
    Review
  19. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  20. Structural identification of catalytic His158 of PtMAC2p fromFrontiers in bioengineering and biotechnology · 2023
    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

5 authors at 2 institutions in 1 country.

Dale F KreitlerDepartment of Structural Biology, Jacobs School of Medicine & Biomedical Sciences at the University at Buffalo, 955 Main Street, Buffalo, NY, 14203, USA.ORCID http://orcid.org/0000-0003-4758-7913
Erin M GemmellDepartment of Chemistry, Washington University in St. Louis, One Brookings Drive, St. Louis, MO, 63130, USA.ORCID http://orcid.org/0000-0001-5305-2080
Jason E SchafferDepartment of Chemistry, Washington University in St. Louis, One Brookings Drive, St. Louis, MO, 63130, USA.
Timothy A WencewiczDepartment of Chemistry, Washington University in St. Louis, One Brookings Drive, St. Louis, MO, 63130, USA. wencewicz@wustl.edu.ORCID http://orcid.org/0000-0002-5839-6672
Andrew M GulickDepartment of Structural Biology, Jacobs School of Medicine & Biomedical Sciences at the University at Buffalo, 955 Main Street, Buffalo, NY, 14203, USA. amgulick@buffalo.edu.ORCID http://orcid.org/0000-0003-4238-7453
Washington University in St. Louis · USUniversity at Buffalo, State University of New York · US

Funding

High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
The Structural Basis for Modular Nonribosomal Peptide SynthesisR01GM116957 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI GULICK, ANDREW M · 2016 to 2019
$1.5M
NIGMS NIH HHS R01 GM116957NIH HHS S10 OD012289
6 · The paper itself

Abstract

Nonribosomal peptide synthetases produce diverse natural products using a multidomain architecture where the growing peptide, attached to an integrated carrier domain, is delivered to neighboring catalytic domains for bond formation and modification. Investigation of these systems can lead to the discovery of new structures, unusual biosynthetic transformations, and to the engineering of catalysts for generating new products. The antimicrobial β-lactone obafluorin is produced nonribosomally from dihydroxybenzoic acid and a β-hydroxy amino acid that cyclizes into the β-lactone during product release. Here we report the structure of the nonribosomal peptide synthetase ObiF1, highlighting the structure of the β-lactone-producing thioesterase domain and an interaction between the C-terminal MbtH-like domain with an upstream adenylation domain. Biochemical assays examine catalytic promiscuity, provide mechanistic insight, and demonstrate utility for generating obafluorin analogs. These results advance our understanding of the structural cycle of nonribosomal peptide synthetases and provide insights into the production of β-lactone natural products.

Indexed as

Biosynthetic PathwaysBurkholderiaCatalytic DomainCrystallography, X-RayLactonesModels, MolecularPeptide SynthasesLactonesnon-ribosomal peptide synthaseobafluorinPeptide Synthases

Identifiers

PMID31366889
PMCPMC6668435
OpenAlexW2963930213

What OpenQuestion holds

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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.