Evidence map›Paper›PMID 17222187›Full record

ArticleThe FEBS journal2007

Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates.

Ramasubramanian Sundaramoorthy, Jorge Iulek, Michael P Barrett, Olivier Bidet, Gian Filippo Ruda, Ian H Gilbert, William N Hunter

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The FEBS journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Crystal Structures of 6-Phosphogluconate Dehydrogenase fromJournal of microbiology and biotechnology · 2023
    Article
  5. Structure ofInternational journal of molecular sciences · 2023
    Article
  6. 6-Phosphogluconate dehydrogenase and its crystal structures.Acta crystallographica. Section F, Structural biology communications · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  14. 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

7 authors at 4 institutions in 2 countries.

Ramasubramanian SundaramoorthyDivision of Biological Chemistry and Molecular Microbiology, College of Life Sciences, University of Dundee, UK.
Jorge Iulek
Michael P Barrett
Olivier Bidet
Gian Filippo Ruda
Ian H Gilbert
William N Hunter
University of Dundee · GBCardiff University · GBUniversidade Estadual de Ponta Grossa · BRUniversity of Glasgow · GB

Funding

Wellcome Trust 075277
6 · The paper itself

Abstract

Crystal structures of recombinant Lactococcus lactis 6-phosphogluconate dehydrogenase (LlPDH) in complex with substrate, cofactor, product and inhibitors have been determined. LlPDH shares significant sequence identity with the enzymes from sheep liver and the protozoan parasite Trypanosoma brucei for which structures have been reported. Comparisons indicate that the key residues in the active site are highly conserved, as are the interactions with the cofactor and the product ribulose 5-phosphate. However, there are differences in the conformation of the substrate 6-phosphogluconate which may reflect distinct states relevant to catalysis. Analysis of the complex formed with the potent inhibitor 4-phospho-d-erythronohydroxamic acid, suggests that this molecule does indeed mimic the high-energy intermediate state that it was designed to. The analysis also identified, as a contaminant by-product of the inhibitor synthesis, 4-phospho-d-erythronamide, which binds in similar fashion. LlPDH can now serve as a model system for structure-based inhibitor design targeting the enzyme from Trypanosoma species.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalysisCoenzymesCrystallography, X-RayEnzyme InhibitorsHydroxamic AcidsLactococcus lactisModels, MolecularMolecular Sequence DataPhosphogluconate DehydrogenaseProtein ConformationSubstrate SpecificitySugar PhosphatesTrypanosoma brucei brucei4-phosphoerythronamide4-phosphoerythronohydroxamic acidCoenzymesEnzyme Inhibitorserythronohydroxamic acidHydroxamic AcidsPhosphogluconate DehydrogenaseSugar Phosphates

Identifiers

PMID17222187
PMCPMC6927799
OpenAlexW1527573530

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.