ArticleProceedings of the National Academy of Sciences of the United States of America1994
Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
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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.
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Who cites it
58 citing papers in PubMed, 132 citations in OpenAlex.
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- Fosfomycin Uptake inACS infectious diseases · 2024Article
- In silico bioprospecting of receptors associated with the mechanism of action of Rondonin, an antifungal peptide from spiderIn silico pharmacology · 2024Article
- Role of internal loop dynamics in antibiotic permeability of outer membrane porins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Outer Membrane Protein F Is Involved in Biofilm Formation, Virulence and Antibiotic Resistance inMicroorganisms · 2021Article
- Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.The EMBO journal · 2021Article
- SecY-mediated quality control prevents the translocation of non-gated porins.Scientific reports · 2020Article
- Transmembrane Epitope Delivery by Passive Protein Threading through the Pores of the OmpF Porin Trimer.Journal of the American Chemical Society · 2020Article
- Engineering bacterial symbionts of nematodes improves their biocontrol potential to counter the western corn rootworm.Nature biotechnology · 2020Article
- Bacteriocins to Thwart Bacterial Resistance in Gram Negative Bacteria.Frontiers in microbiology · 2020Review
- Microcins inFrontiers in microbiology · 2019Review
- PoreDesigner for tuning solute selectivity in a robust and highly permeable outer membrane pore.Nature communications · 2018Article
- The fitness costs and trade-off shapes associated with the exclusion of nine antibiotics by OmpF porin channels.The ISME journal · 2017Article
- Molecular Basis of Filtering Carbapenems by Porins from β-Lactam-resistant Clinical Strains of Escherichia coli.The Journal of biological chemistry · 2016Article
- How Porin Heterogeneity and Trade-Offs Affect the Antibiotic Susceptibility of Gram-Negative Bacteria.Genes · 2015Article
- Article
- Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A strain of Escherichia coli, selected on the basis of its resistance to colicin N, reveals distinct structural and functional alterations in unspecific OmpF porin. A single mutation [Gly-119-->Asp (G119D)] was identified in the internal loop L3 that contributes critically to the formation of the construction inside the lumen of the pore. X-ray structure analysis to a resolution of 3.0 A reveals a locally altered peptide backbone, with the side chain of residue Asp-119 protruding into the channel, causing the area of the constriction (7 x 11 A in the wild type) to be subdivided into two intercommunicating subcompartments of 3-4 A in diameter. The functional consequences of this structural modification consist of a reduction of the channel conductance by about one-third, of altered ion selectivity and voltage gating, and of a decrease of permeation rates of various sugars by factors of 2-12. The structural modification of the mutant protein affects neither the beta-barrel structure nor those regions of the molecule that are exposed at the cell surface. Considering the colicin resistance of the mutant, it is inferred that in vivo, colicin N traverses the outer membrane through the porin channel or that the dynamics of the exposed loops are affected in the mutant such that these may impede the binding of the toxin.
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Registered trials
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.