6GNZ
Plantaricin S-a in 100 mM DPC micelles. This is the alpha part of the bacteriocin plantaricin S.
Summary for 6GNZ
| Entry DOI | 10.2210/pdb6gnz/pdb |
| NMR Information | BMRB: 34278 |
| Descriptor | Plantaricin S alpha protein (1 entity in total) |
| Functional Keywords | antimicrobial protein bacteriocin menbrane interacting peptide, antimicrobial protein |
| Biological source | Lactobacillus plantarum |
| Total number of polymer chains | 1 |
| Total formula weight | 2926.44 |
| Authors | Ekblad, B.,Kristiansen, P.E. (deposition date: 2018-06-01, release date: 2019-03-06, Last modification date: 2024-06-19) |
| Primary citation | Ekblad, 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: 30787405DOI: 10.1038/s41598-019-38518-6 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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