ArticleApplied and environmental microbiology2008
Mutational analysis of the class IIa bacteriocin curvacin A and its orientation in target cell membranes.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Characterization of a Bacteriocin-like Substance fromVeterinary sciences · 2026Article
- Synthesis, antimicrobial activity and conformational analysis of the class IIa bacteriocin pediocin PA-1 and analogs thereof.Scientific reports · 2018Article
- LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor.Applied and environmental microbiology · 2016Article
- Bacteriocins of lactic acid bacteria: extending the family.Applied microbiology and biotechnology · 2016Review
- Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1.Applied and environmental microbiology · 2011Article
- Insights into the functionality of the putative residues involved in enterocin AS-48 maturation.Applied and environmental microbiology · 2010Article
- Synthesis of trypsin-resistant variants of the Listeria-active bacteriocin salivaricin P.Applied and environmental microbiology · 2010Article
- Helix insertion into bilayers and the evolution of membrane proteins.Cellular and molecular life sciences : CMLS · 2010Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To analyze the orientation in target cell membranes of the pediocin-like bacteriocin (antimicrobial peptide) curvacin A, 55 variants were generated by site-directed mutagenesis and their potencies against four different target cells determined. The result suggest that the somewhat hydrophilic short central helix (residues 19 to 24), along with the N-terminal beta-sheet-like structure (residues 1 to 16), inserts in the interface region of the target cell membrane, with Ala22 close to the hydrophobic core of the membrane. The following hinge region, with Gly28 as an important residue, may then form a turn wherein Gly28 becomes positioned near the border between the interface and the hydrophobic regions, thus permitting the longer and more-hydrophobic C-terminal helix (residues 29 to 41) to insert into the hydrophobic core of the membrane. This helix contains three glycine residues (G33, G37, and G40) that form a putative helix-helix-interacting GxxxGxxG motif. The replacement of any of these glycines with a larger residue was very detrimental, suggesting their possible involvement in helix-helix interactions with a membrane-embedded receptor protein.
Indexed as
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What OpenQuestion holds
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.