Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF

• Published in: Biochimica et biophysica acta 2008-11, Vol.1784 (11), p.1711-1719
• Main Authors: Fimland, Nina, Rogne, Per, Fimland, Gunnar, Nissen-Meyer, Jon, Kristiansen, Per Eugen
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Antimicrobial peptide; Bacteria; Bacteriocins - chemistry; Bacteriocins - isolation & purification; Lactic acid bacteria; Models, Molecular; Molecular Conformation; Molecular Sequence Data; NMR spectroscopy; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments - chemistry; Peptide Fragments - isolation & purification; Peptide structure; Plantaricin EF; Structural Homology, Protein
• ISSN: 1570-9639; 0006-3002; 1878-1454
• DOI: 10.1016/j.bbapap.2008.05.003

The three-dimensional structures of the two peptides plantaricin E (plnE; 33 residues) and plantaricin F (plnF; 34 residues) constituting the two-peptide bacteriocin plantaricin EF (plnEF) have been determined by nuclear magnetic resonance (NMR) spectroscopy in the presence of DPC micelles. PlnE has an N-terminal α-helix (residues 10–21), and a C-terminal α-helix-like structure (residues 25–31). PlnF has a long central α-helix (residues 7–32) with a kink of 38 ± 7 degrees at Pro20. There is some flexibility in the helix in the kink region. Both helices in plnE are amphiphilic, while the helix in plnF is polar in its N-terminal half and amphiphilic in its C-terminal half. The α-helical content obtained by NMR spectroscopy is in agreement with CD studies. PlnE has two GxxxG motifs which are putative helix–helix interaction motifs, one at residues 5 to 9 and one at residues 20 to 24, while plnF has one such motif at residues 30 to 34. The peptides are flexible in these GxxxG regions. It is suggested that the two peptides lie parallel in a staggered fashion relative to each other and interact through helix–helix interactions involving the GxxxG motifs.