Evidence map›Paper›PMID 35347220›Full record

ArticleCommunications biology2022

Molecular basis of specificity and deamidation of eIF4A by Burkholderia Lethal Factor 1.

George W Mobbs, Adli A Aziz, Samuel R Dix, G M Blackburn, Sveta E Sedelnikova, Thomas C Minshull, Mark J Dickman, Patrick J Baker, Sheila Nathan, Mohd Firdaus Raih and 1 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Structural insights into a putative BLF1-like deamidase from Methylomonas sp. Kb3.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Article
  3. Article
  4. Burkholderia pseudomallei and melioidosis.Nature reviews. Microbiology · 2024
    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

11 authors at 5 institutions in 3 countries.

George W Mobbs *Krebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0003-2405-3345
Adli A Aziz *Krebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0002-2665-2467
Samuel R Dix *Krebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0002-6907-1435
G M BlackburnKrebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.
Sveta E SedelnikovaKrebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.
Thomas C MinshullDepartment of Chemical and Biological Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK.
Mark J DickmanDepartment of Chemical and Biological Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK.ORCID http://orcid.org/0000-0002-9236-0788
Patrick J BakerKrebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0003-1995-5643
Sheila NathanDepartment of Biological Sciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600, UKM Bangi, Bangi, Selangor, Malaysia.ORCID http://orcid.org/0000-0002-2132-2346
Mohd Firdaus RaihDepartment of Applied Physics, Faculty of Science and Technology and Institute of Systems Biology, Universiti Kebangsaan Malaysia, 43600, UKM Bangi, Bangi, Selangor, Malaysia.
David W RiceKrebs Institute, School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK. d.rice@sheffield.ac.uk.ORCID http://orcid.org/0000-0002-7811-0539
University of Sheffield · GBNational University of Malaysia · MYCalifornia Institute of Technology · USMalaysia Theological Seminary · MYUniversity of Leeds · GB

Funding

Diamond Light Source MX17773Diamond Light Source MX8987RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M012166/1Royal Society IC170306
6 · The paper itself

Abstract

Burkholderia pseudomallei lethal factor 1 (BLF1) exhibits site-specific glutamine deamidase activity against the eukaryotic RNA helicase, eIF4A, thereby blocking mammalian protein synthesis. The structure of a complex between BLF1 C94S and human eIF4A shows that the toxin binds in the cleft between the two RecA-like eIF4A domains forming interactions with residues from both and with the scissile amide of the target glutamine, Gln339, adjacent to the toxin active site. The RecA-like domains adopt a radically twisted orientation compared to other eIF4A structures and the nature and position of conserved residues suggests this may represent a conformation associated with RNA binding. Comparison of the catalytic site of BLF1 with other deamidases and cysteine proteases reveals that they fall into two classes, related by pseudosymmetry, that present either the re or si faces of the target amide/peptide to the nucleophilic sulfur, highlighting constraints in the convergent evolution of their Cys-His active sites.

Indexed as

BurkholderiaEukaryotic Initiation Factor-4AAmidesAnimalsGlutamineHumansMammalsProtein BiosynthesisAmidesEukaryotic Initiation Factor-4AGlutamine

Identifiers

PMID35347220
PMCPMC8960835
OpenAlexW4220803793

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.