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6GO0

PLANTARICIN S-B IN 100 MM DPC MICELLES. THIS IS THE BETA PART OF THE BACTERIOCIN PLANTARICIN S

Summary for 6GO0
Entry DOI10.2210/pdb6go0/pdb
NMR InformationBMRB: 34279
DescriptorPlantaricin S beta protein (1 entity in total)
Functional Keywordsantimicrobial protein bacteriocin menbrane interacting peptide, antimicrobial protein
Biological sourceLactobacillus plantarum
Total number of polymer chains1
Total formula weight2877.26
Authors
Ekblad, B.,Kristiansen, P.E. (deposition date: 2018-06-01, release date: 2019-03-06, Last modification date: 2024-06-19)
Primary citationEkblad, B.,Kristiansen, P.E.
NMR structures and mutational analysis of the two peptides constituting the bacteriocin plantaricin S.
Sci Rep, 9:2333-2333, 2019
Cited by
PubMed Abstract: 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-α and Pls-β, form an α-helix from and including residue 8 to 24 with a less structured region around residue 16-19 and an amphiphilic α-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 GxxxG motif in Pls-α and the SxxxG motif in Pls-β 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.
PubMed: 30787405
DOI: 10.1038/s41598-019-38518-6
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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