ArticleProceedings of the National Academy of Sciences of the United States of America2000
Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
- The DdD protein confers intracellular and extracellular immunity to the leaderless bacteriocin enterocin DD14.PNAS nexus · 2026Article
- PERSISTENT SHEAF LAPLACIANS.Foundations of data science (Springfield, Mo.) · 2025Article
- From In Vitro Promise to In Vivo Reality: An Instructive Account of Infection Model Evaluation of Antimicrobial Peptides.International journal of molecular sciences · 2024Article
- Tertiary Plasticity Drives the Efficiency of Enterocin 7B Interactions with Lipid Membranes.The journal of physical chemistry. B · 2024Article
- Production of Pumilarin and a Novel Circular Bacteriocin, Altitudin A, byInternational journal of molecular sciences · 2024Article
- Antimicrobial Peptides (AMPs): Potential Therapeutic Strategy against Trypanosomiases?Biomolecules · 2023Review
- Classification and Multifaceted Potential of Secondary Metabolites Produced byMolecules (Basel, Switzerland) · 2023Review
- Advances in the preclinical characterization of the antimicrobial peptide AS-48.Frontiers in microbiology · 2023Review
- Rationally Designed Minimal Bioactive Domains of AS-48 Bacteriocin Homologs Possess Potent Antileishmanial Properties.Microbiology spectrum · 2022Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Peptide/protein-based macrocycles: from biological synthesis to biomedical applications.RSC chemical biology · 2022Review
- The Role of Key Amino Acids in the Antimicrobial Mechanism of a Bacteriocin Model Revealed by Molecular Simulations.Journal of chemical information and modeling · 2021Article
- A glutamic acid-based traceless linker to address challenging chemical protein syntheses.Organic & biomolecular chemistry · 2021Article
- Mechanisms of action of ribosomally synthesized and posttranslationally modified peptides (RiPPs).Journal of industrial microbiology & biotechnology · 2021Review
- A chameleonic macrocyclic peptide with drug delivery applications.Chemical science · 2021Article
- Crystal structure and site-directed mutagenesis of circular bacteriocin plantacyclin B21AG reveals cationic and aromatic residues important for antimicrobial activity.Scientific reports · 2020Article
- Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.iScience · 2020Article
- Bioinformatic prospecting and phylogenetic analysis reveals 94 undescribed circular bacteriocins and key motifs.BMC microbiology · 2020Article
- The role of disulfide bonds in a Solanum tuberosum saposin-like protein investigated using molecular dynamics.PloS one · 2020Article
- Synthetic Peptide Libraries Designed From a Minimal Alpha-Helical Domain of AS-48-Bacteriocin Homologs Exhibit Potent Antibacterial Activity.Frontiers in microbiology · 2020Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The solution structure of bacteriocin AS-48, a 70-residue cyclic polypeptide from Enterococcus faecalis, consists of a globular arrangement of five alpha-helices enclosing a compact hydrophobic core. The head-to-tail union lies in the middle of helix 5, a fact that is shown to have a pronounced effect on the stability of the three-dimensional structure. Positive charges in the side chains of residues in helix 4 and in the turn linking helix 4 to helix 5 form a cluster that most probably determine its antibacterial activity by promoting pore formation in cell membranes. A similar five-helix structural motif has been found in the antimicrobial NK-lysin, an effector polypeptide of T and natural killer (NK) cells. Bacteriocin AS-48 lacks the three disulfide bridges characteristic of the saposin fold present in NK-lysin, and has no sequence homology with it. Nevertheless, the similar molecular architecture and high positive charge strongly suggest a common mechanism of antibacterial action.
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