Evidence map›Paper›PMID 28481092›Full record

ArticleBiochemistry2017

Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.

Robert L Evans, John A Latham, Youlin Xia, Judith P Klinman, Carrie M Wilmot

Abstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Biosynthesis of Macrocyclic Peptides by Formation and Crosslinking ofbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023
    Review
  7. Article
  8. Article
  9. Substrate Recognition by the Peptidyl-(ACS chemical biology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Review
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  16. 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

5 authors at 2 institutions in 1 country.

Robert L EvansDepartment of Biochemistry, Molecular Biology, and Biophysics and Biotechnology Institute, University of Minnesota, Twin Cities , St. Paul, Minnesota 55108, United States.
John A LathamDepartment of Chemistry and Department of Molecular and Cell Biology, University of California, Berkeley , Berkeley, California 94720, United States.
Youlin XiaMinnesota NMR Center, University of Minnesota, Twin Cities , Minneapolis, Minnesota 55455, United States.
Judith P KlinmanDepartment of Chemistry and Department of Molecular and Cell Biology, University of California, Berkeley , Berkeley, California 94720, United States.ORCID 0000-0001-5734-2843
Carrie M WilmotDepartment of Biochemistry, Molecular Biology, and Biophysics and Biotechnology Institute, University of Minnesota, Twin Cities , St. Paul, Minnesota 55108, United States.ORCID 0000-0002-8706-0000
University of Minnesota · USUniversity of California, Berkeley · US

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
Catalysis and biogenesis in methylamine dehydrogenaseR01GM066569 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WILMOT, CAROLINE MARY · 2002 to 2015
$4.0M
NIGMS NIH HHS R01 GM066569NIGMS NIH HHS R35 GM118117
6 · The paper itself

Abstract

Biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is initiated when the precursor peptide, PqqA, is recognized and bound by the RiPP precursor peptide recognition element (RRE), PqqD, for presentation to the first enzyme in the pathway, PqqE. Unlike other RiPP-producing, postribosomal peptide synthesis (PRPS) pathways in which the RRE is a component domain of the first enzyme, PqqD is predominantly a separate scaffolding protein that forms a ternary complex with the precursor peptide and first tailoring enzyme. As PqqD is a stable, independent RRE, this makes the PQQ pathway an ideal PRPS model system for probing RRE interactions using nuclear magnetic resonance (NMR). Herein, we present both the solution NMR structure of Methylobacterium extorquens PqqD and results of

Indexed as

Nuclear Magnetic Resonance, BiomolecularBacterial ProteinsBinding SitesMethylobacterium extorquensModels, MolecularMolecular ChaperonesOxidoreductasesPQQ CofactorProtein ConformationBacterial ProteinsMolecular ChaperonesOxidoreductasesPQQ CofactorPqqD protein, Methylobacterium extorquens

Identifiers

PMID28481092
PMCPMC5526462
OpenAlexW2612021295

What OpenQuestion holds

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LicenceTDM
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.