Evidence map›Paper›PMID 18824174›Full record

ArticleJournal of molecular biology2008

Three-dimensional structures of Pseudomonas aeruginosa PvcA and PvcB, two proteins involved in the synthesis of 2-isocyano-6,7-dihydroxycoumarin.

Eric J Drake, Andrew M Gulick

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Copper-chelating natural products.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
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  6. Biosynthesis of Isonitrile- and Alkyne-Containing Natural Products.Annual review of chemical and biomolecular engineering · 2022
    Review
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  8. Article
  9. The evolution of virulence inProceedings. Biological sciences · 2020
    Article
  10. Article
  11. Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase.Angewandte Chemie (International ed. in English) · 2018
    Article
  12. Article
  13. Frontiers in microbiology · 2018
    Article
  14. Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. PeerJ · 2016
    Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Eric J DrakeHauptman-Woodward Medical Research Institute, Department of Structural Biology, State University of New York at Buffalo, 700 Ellicott St, Buffalo, NY 14203-1102, USA.
Andrew M Gulick
Hauptman-Woodward Medical Research Institute · US

Funding

Structures of Peptide Synthetases and Related EnzymesR01GM068440 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI GULICK, ANDREW M · 2004 to 2013
$3.1M
NIGMS NIH HHS GM-068440NIGMS NIH HHS R01 GM068440
6 · The paper itself

Abstract

The pvcABCD operon of Pseudomonas aeruginosa encodes four proteins (PA2254, PA2255, PA2256, and PA2257) that form a cluster that is responsible for the synthesis of a cyclized isocyano derivative of tyrosine. These proteins, which were identified originally as being responsible for a step in the maturation of the chromophore of the peptide siderophore pyoverdine, have been identified recently as belonging to a family of proteins that produce small organic isonitriles. We report that strains harboring a disruption in the pvcA or pvcB genes are able to grow in iron-depleted conditions and to produce pyoverdine. Additionally, we have determined the three-dimensional crystal structures of PvcA and PvcB. The structure of PvcA demonstrates a novel enzyme architecture that is built upon a Rossmann fold. We have analyzed the sequence conservation of enzymes within this family and identified six conserved motifs. These regions of the protein cluster around a putative active site cavity. The structure of the PvcB protein confirms it is a member of the Fe2+/alpha-ketoglutarate-dependent oxygenase family of enzymes. The active site of PvcB is compared to the structures of other family members and suggests that a conformational change to order several loops will accompany the binding of ligands.

Indexed as

Amino Acid MotifsAmino Acid SequenceBacterial ProteinsCell ProliferationConserved SequenceCoumarinsCrystallography, X-RayCulture MediaIron Chelating AgentsMolecular Sequence DataMutationOligopeptidesOperonProtein Structure, SecondaryPseudomonas aeruginosaSequence Alignment2-isocyano-6,7-dihydroxycoumarinBacterial ProteinsCoumarinsCulture MediaIron Chelating AgentsOligopeptidespyoverdin

Identifiers

PMID18824174
PMCPMC2701257
OpenAlexW2123180894

What OpenQuestion holds

Textmetadata
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.