• DRAMP ID

    • DRAMP00061
    • Peptide Name

    • Actagardine (Gardimycin; Bacteriocin)
    • Source

    • Actinoplanes liguriae (Gram-positive bacteria)
    • Family

    • Belongs to the type B lantibiotic family (Class I bacteriocin)
    • Gene

    • N/A
    • Sequence

    • ASGWVCTLTIECGTVICAC
    • Sequence Length

    • 19
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Anti-Gram+, Antimicrobial
    • Target Organism

      • Gram-positive bacteria: streptococci, Streptococcus pyogenes.
    • Hemolytic Activity

      • N/A
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Lipid II
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Other Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Non helix or strand structure
    • Structure Description

    • Actagardine shows a rigid compact globular shape based on the constraining bridging pattern, which is composed of an N-terminal lanthionine ring from residues 1-6 and three intertwined C-terminal methyllanthionine rings comprising residues 7-12, 9-17 and 14-19. In addition, this C-terminal ring system is stabilised by a short antiparallel beta sheet. A feature of the actagardine structure is the presence of two putative binding pockets.
    • PDB ID

    • 1AJ1 resolved by NMR.
    • DRAMP00061 helical wheel diagram
    • 1AJ1-> 
    • Formula

    • C81H132N20O26S4
    • Absent Amino Acids

    • DFHKMNPQRY
    • Common Amino Acids

    • C
    • Mass

    • 2251.57
    • PI

    • 3.85
    • Basic Residues

    • 0
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 8
    • Boman Index

    • 17.87
    • Hydrophobicity

    • 140.53
    • Aliphatic Index

    • 102.63
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5750
    • Absorbance 280nm

    • 319.44
    • Polar Residues

    • 10

DRAMP00061

DRAMP00061 chydropathy plot
    • Function

    • The molecule has a compact shape. Like mersacidin, this peptide inhibits cell wall biosynthesis by binding to lipid II.
    • PTM

    • Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The 14-19 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor.
  • Literature 1
    • Title

    • Sequence determination of actagardine, a novel lantibiotic, by homonuclear 2D NMR spectroscopy.
    • Reference

    • J Antibiot (Tokyo). 1990 Sep;43(9):1082-1088.
    • Author

    • Kettenring JK, Malabarba A, V©key K, Cavalleri B.
  • Literature 2
    • Title

    • The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR.
    • Reference

    • Eur J Biochem. 1997 Jun 15;246(3):809-819.
    • Author

    • Zimmermann N, Jung G.