Evidence map›Paper›PMID 37114973›Full record

ReviewNatural product reports2023

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.

Ketan D Patel, Monica R MacDonald, Syed Fardin Ahmed, Jitendra Singh, Andrew M Gulick

Open access · hybridAbstract readReview
In one paragraph

Review in Natural product reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

30 citing papers in PubMed, 45 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Ketan D PatelUniversity at Buffalo, Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, 55 Main St. Buffalo, NY 14203, USA. amgulick@buffalo.edu.ORCID 0000-0003-4254-3145
Monica R MacDonaldUniversity at Buffalo, Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, 55 Main St. Buffalo, NY 14203, USA. amgulick@buffalo.edu.ORCID 0000-0002-9325-8291
Syed Fardin AhmedUniversity at Buffalo, Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, 55 Main St. Buffalo, NY 14203, USA. amgulick@buffalo.edu.ORCID 0000-0002-9994-4022
Jitendra SinghUniversity at Buffalo, Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, 55 Main St. Buffalo, NY 14203, USA. amgulick@buffalo.edu.ORCID 0000-0002-5257-1337
Andrew M GulickUniversity at Buffalo, Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, 55 Main St. Buffalo, NY 14203, USA. amgulick@buffalo.edu.ORCID 0000-0003-4238-7453
University at Buffalo, State University of New York · US

Funding

Structural Studies of Nonribosomal Peptide SynthesisR35GM136235 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI GULICK, ANDREW M · 2020 to 2024
$2.0M
NIGMS NIH HHS R35 GM136235
6 · The paper itself

Abstract

Covering: up to fall 2022.Nonribosomal peptide synthetases (NRPSs) are a family of modular, multidomain enzymes that catalyze the biosynthesis of important peptide natural products, including antibiotics, siderophores, and molecules with other biological activity. The NRPS architecture involves an assembly line strategy that tethers amino acid building blocks and the growing peptides to integrated carrier protein domains that migrate between different catalytic domains for peptide bond formation and other chemical modifications. Examination of the structures of individual domains and larger multidomain proteins has identified conserved conformational states within a single module that are adopted by NRPS modules to carry out a coordinated biosynthetic strategy that is shared by diverse systems. In contrast, interactions between modules are much more dynamic and do not yet suggest conserved conformational states between modules. Here we describe the structures of NRPS protein domains and modules and discuss the implications for future natural product discovery.

Indexed as

PeptidesPeptide SynthasesCatalytic DomainProtein Domainsnon-ribosomal peptide synthasePeptidesPeptide Synthases

Identifiers

PMID37114973
PMCPMC10510592
OpenAlexW4367320887

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.