Evidence map›Paper›PMID 23527057›Full record

ArticlePloS one2013

The structure of HasB reveals a new class of TonB protein fold.

Gisele Cardoso de Amorim, Ada Prochnicka-Chalufour, Philippe Delepelaire, Julien Lefèvre, Catherine Simenel, Cécile Wandersman, Muriel Delepierre, Nadia Izadi-Pruneyre

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020
    Review
  11. Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2019
    Review
  12. Article
  13. Article
  14. Degradation of dexamethasone by acclimated strain of Pseudomonas Alcaligenes.International journal of clinical and experimental medicine · 2015
    Article
  15. Heme uptake in bacterial pathogens.Current opinion in chemical biology · 2014
    Review
  16. Article
  17. 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

8 authors at 4 institutions in 1 country.

Gisele Cardoso de AmorimInstitut Pasteur, Unité de Résonance Magnétique Nucléaire des Biomolécules, Département de Biologie Structurale et Chimie, Paris, France.
Ada Prochnicka-Chalufour
Philippe Delepelaire
Julien Lefèvre
Catherine Simenel
Cécile Wandersman
Muriel Delepierre
Nadia Izadi-Pruneyre
Centre National de la Recherche Scientifique · FRInstitut Pasteur · FRLaboratoire des Biomolécules · FRInstitut de Biologie Physico-Chimique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TonB is a key protein in active transport of essential nutrients like vitamin B12 and metal sources through the outer membrane transporters of Gram-negative bacteria. This inner membrane protein spans the periplasm, contacts the outer membrane receptor by its periplasmic domain and transduces energy from the cytoplasmic membrane pmf to the receptor allowing nutrient internalization. Whereas generally a single TonB protein allows the acquisition of several nutrients through their cognate receptor, in some species one particular TonB is dedicated to a specific system. Despite a considerable amount of data available, the molecular mechanism of TonB-dependent active transport is still poorly understood. In this work, we present a structural study of a TonB-like protein, HasB dedicated to the HasR receptor. HasR acquires heme either free or via an extracellular heme transporter, the hemophore HasA. Heme is used as an iron source by bacteria. We have solved the structure of the HasB periplasmic domain of Serratia marcescens and describe its interaction with a critical region of HasR. Some important differences are observed between HasB and TonB structures. The HasB fold reveals a new structural class of TonB-like proteins. Furthermore, we have identified the structural features that explain the functional specificity of HasB. These results give a new insight into the molecular mechanism of nutrient active transport through the bacterial outer membrane and present the first detailed structural study of a specific TonB-like protein and its interaction with the receptor.

Indexed as

Protein FoldingAmino AcidsAmino Acid SequenceBacterial ProteinsBinding SitesMembrane ProteinsModels, MolecularMolecular Sequence DataPeptidesProtein BindingProtein ConformationProtein Structure, SecondarySequence AlignmentAmino AcidsBacterial ProteinsHasB protein, Serratia marcescensMembrane ProteinsPeptidestonB protein, Bacteria

Identifiers

PMID23527057
PMCPMC3602595
OpenAlexW2067469603

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.