General Information

    • 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

    • Not found

    • Sequence

    • ASGWVCTLTIECGTVICAC

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

      • Gram-positive bacteria: streptococci, Streptococcus pyogenes.

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Lipid II

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal 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.

    • Helical Wheel Diagram

    • DRAMP00061 helical wheel diagram

    • PDB ID

    • 1AJ1 resolved by NMR.
  • 1AJ1-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP00061.

Physicochemical Information

    • Formula

    • C81H132N20O26S4

    • Absent Amino Acids

    • DFHKMNPQRY

    • Common Amino Acids

    • C

    • Mass

    • 1930.3

    • PI

    • 4

    • Basic Residues

    • 0

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 8

    • Net Charge

    • -1

    • Boman Index

    • 17.87

    • Hydrophobicity

    • 1.405

    • 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

Comments Information

    • 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 Information

  • ·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.