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Publication Abstract from PubMed

The structure of the individual peptides of the two-peptide bacteriocin plantaricin S, an antimicrobial peptide produced by a Lactobacillus plantarum strain, has been determined in DPC micelles. The two peptides of plantaricin S, Pls-alpha and Pls-beta, form an alpha-helix from and including residue 8 to 24 with a less structured region around residue 16-19 and an amphiphilic alpha-helix from and including residue 7 to 23, respectively. Activity assays on single amino acid-substituted GxxxG and GxxxG-like motifs show that substituting the Ser and Gly residues in the G9xxxG13 motif in Pls-alpha and the S17xxxG21 motif in Pls-beta reduced or drastically reduced the antimicrobial activity. The two-peptide bacteriocin muricidin contains GxxxG-like motifs at similar positions and displays 40-50% amino acid identity with plantaricin S. Activity assays of combinations of the peptides that constitute the bacteriocins plantaricin S and muricidin show that some combinations are highly active. Furthermore, sequence alignments show that the motifs important for plantaricin S activity align with identical motifs in muricidin. Based on sequence comparison and activity assays, a membrane-inserted model of plantaricin S in which the two peptides are oriented antiparallel relative to each other and where the GxxxG and GxxxG-like motifs important for activity come close in space, is proposed.

NMR structures and mutational analysis of the two peptides constituting the bacteriocin plantaricin S.,Ekblad B, Kristiansen PE Sci Rep. 2019 Feb 20;9(1):2333. doi: 10.1038/s41598-019-38518-6. PMID:30787405^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.