Evidence map›Paper›PMID 21124774›Full record

ArticlePloS one2010

The crystal structure of OprG from Pseudomonas aeruginosa, a potential channel for transport of hydrophobic molecules across the outer membrane.

Debra S Touw, Dimki R Patel, Bert van den Berg

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-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

29 citing papers in PubMed, 65 citations in OpenAlex.

  1. From Environmental Organism to Nosocomial Threat:Antibiotics (Basel, Switzerland) · 2026
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  2. Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026
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  5. Evaluation ofFrontiers in microbiology · 2023
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  9. Microorganisms · 2022
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  12. A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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

3 authors at 1 institution in 1 country.

Debra S TouwProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Dimki R Patel
Bert van den Berg
University of Massachusetts Chan Medical School · US

Funding

Structural and biochemical characterization of the OprD membrane protein familyR01GM085785 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI VAN DEN BERG, BERT · 2008 to 2011
$1.3M
NIGMS NIH HHS 5R01GM085785NIGMS NIH HHS R01 GM085785
6 · The paper itself

Abstract

backgroundThe outer membrane (OM) of Gram-negative bacteria provides a barrier to the passage of hydrophobic and hydrophilic compounds into the cell. The OM has embedded proteins that serve important functions in signal transduction and in the transport of molecules into the periplasm. The OmpW family of OM proteins, of which P. aeruginosa OprG is a member, is widespread in Gram-negative bacteria. The biological functions of OprG and other OmpW family members are still unclear. METHODOLOGY/PRINCIPAL

findingsIn order to obtain more information about possible functions of OmpW family members we have solved the X-ray crystal structure of P. aeruginosa OprG at 2.4 Å resolution. OprG forms an eight-stranded β-barrel with a hydrophobic channel that leads from the extracellular surface to a lateral opening in the barrel wall. The OprG barrel is closed off from the periplasm by interacting polar and charged residues on opposite sides of the barrel wall. CONCLUSIONS/SIGNIFICANCE: The crystal structure, together with recent biochemical data, suggests that OprG and other OmpW family members form channels that mediate the diffusion of small hydrophobic molecules across the OM by a lateral diffusion mechanism similar to that of E. coli FadL.

Indexed as

Models, BiologicalBacterial Outer Membrane ProteinsBiological TransportCell MembraneCrystallography, X-RayHydrophobic and Hydrophilic InteractionsIon ChannelsModels, MolecularPeriplasmProtein ConformationProtein Structure, TertiaryBacterial Outer Membrane ProteinsIon ChannelsOprG protein, Pseudomonas aeruginosa

Identifiers

PMID21124774
PMCPMC2993939
OpenAlexW2066900950

What OpenQuestion holds

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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.