Evidence map›Paper›PMID 18583986›Full record

ArticleEMBO reports2008

The nature and character of the transition state for the ADP-ribosyltransferase reaction.

René Jørgensen, Yolanda Wang, Danielle Visschedyk, A Rod Merrill

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
1.5field-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

53 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  10. Cells · 2023
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  12. Apprehending the NADViruses · 2022
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  15. Article
  16. Article
  17. Article
  18. Review
  19. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    Review
  20. Review
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.

René JørgensenDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada.
Yolanda Wang
Danielle Visschedyk
A Rod Merrill
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exotoxin A (ExoA) from Pseudomonas aeruginosa is an important virulence factor that belongs to a class of exotoxins that are secreted by pathogenic bacteria which cause human diseases such as cholera, diphtheria, pneumonia and whooping cough. We present the first crystal structures, to our knowledge, of ExoA in complex with elongation factor 2 (eEF2) and intact NAD(+), which indicate a direct role of two active-site loops in ExoA during the catalytic cycle. One loop moves to form a solvent cover for the active site of the enzyme and reaches towards the target residue (diphthamide) in eEF2 forming an important hydrogen bond. The NAD(+) substrate adopts a conformation remarkably different from that of the NAD(+) analogue, betaTAD, observed in previous structures, and fails to trigger any loop movements. Mutational studies of the two loops in the toxin identify several residues important for catalytic activity, in particular Glu 546 and Arg 551, clearly supporting the new complex structures. On the basis of these data, we propose a transition-state model for the toxin-catalysed reaction.

Indexed as

ADP Ribose TransferasesBacterial ToxinsCrystallography, X-RayExotoxinsHumansModels, MolecularMutagenesis, Site-DirectedMutationNADPeptide Elongation Factor 2Protein BindingProtein Structure, SecondaryPseudomonas aeruginosaPseudomonas aeruginosa Exotoxin AStructure-Activity RelationshipVirulence FactorsADP Ribose TransferasesBacterial ToxinsExotoxinsNADPeptide Elongation Factor 2Pseudomonas aeruginosa Exotoxin AVirulence Factors

Identifiers

PMID18583986
PMCPMC2515215
OpenAlexW2171783362

What OpenQuestion holds

Textmetadata
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.