Evidence map›Paper›PMID 26340431›Full record

ArticleJournal of the American Chemical Society2015

Structure and Substrate Sequestration in the Pyoluteorin Type II Peptidyl Carrier Protein PltL.

Matt J Jaremko, D John Lee, Stanley J Opella, Michael D Burkart

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. 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
7.3field-weighted citation impact, top 3% 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, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Probing Substrate-Loaded Carrier Proteins by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. NMR as a readout to monitor and restore the integrity of complex chemoenzymatic reactions.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    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

4 authors at 1 institution in 1 country.

Matt J JaremkoDepartment of Chemistry and Biochemistry, University of California, San Diego , 9500 Gilman Drive, La Jolla, California 92093-0358, United States.
D John LeeDepartment of Chemistry and Biochemistry, University of California, San Diego , 9500 Gilman Drive, La Jolla, California 92093-0358, United States.
Stanley J OpellaDepartment of Chemistry and Biochemistry, University of California, San Diego , 9500 Gilman Drive, La Jolla, California 92093-0358, United States.
Michael D BurkartDepartment of Chemistry and Biochemistry, University of California, San Diego , 9500 Gilman Drive, La Jolla, California 92093-0358, United States.
University of California, San Diego · US

Funding

RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Contemporary Approaches to Cancer Cell Signaling and CommunicationT32CA009523 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DONOGHUE, DANIEL J, YANG, JING · 1985 to 2025
$12.1M
Protein-Protein Interactions in Natural Product BiosynthesisR01GM095970 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2012 to 2025
$5.9M
NCI NIH HHS T32 CA009523NIBIB NIH HHS P41 EB002031NIGMS NIH HHS GM095970NIGMS NIH HHS R01 GM095970
6 · The paper itself

Abstract

Type II nonribosomal peptide synthetases (NRPS) generate exotic amino acid derivatives that, combined with additional pathways, form many bioactive natural products. One family of type II NRPSs produce pyrrole moieties, which commonly arise from proline oxidation while tethered to a conserved, type II peptidyl carrier protein (PCP), as exemplified by PltL in the biosynthesis of pyoluteorin. We sought to understand the structural role of pyrrole PCPs in substrate and protein interactions through the study of pyrrole analogs tethered to PltL. Solution-phase NMR structural analysis revealed key interactions in residues of helix II and III with a bound pyrrole moiety. Conservation of these residues among PCPs in other pyrrole containing pathways suggests a conserved mechanism for formation, modification, and incorporation of pyrrole moieties. Further NOE analysis provided a unique pyrrole binding motif, offering accurate substrate positioning within the cleft between helices II and III. The overall structure resembles other PCPs but contains a unique conformation for helix III. This provides evidence of sequestration by the PCP of aromatic pyrrole substrates, illustrating the importance of substrate protection and regulation in type II NRPS systems.

Indexed as

Magnetic Resonance SpectroscopyModels, MolecularPhenolsPhospholipid Transfer ProteinsProtein ConformationPyrrolesPhenolsPhospholipid Transfer ProteinspyoluteorinPyrroles

Identifiers

PMID26340431
PMCPMC4847951
OpenAlexW1243774613

What OpenQuestion holds

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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.