• DRAMP ID

    • DRAMP02901
    • Peptide Name

    • Tricyclic peptide MS-271
    • Source

    • Streptomyces sp.
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • CLGVGSCNNFAGCGYAIVCFW
    • Sequence Length

    • 21
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus, Enterococcus faecium.
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Not found
    • 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

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP02901 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02901.
    • Formula

    • C97H138N24O26S4
    • Absent Amino Acids

    • DEHKMPQRT
    • Common Amino Acids

    • CG
    • Mass

    • 2184.55
    • PI

    • 5.5
    • Basic Residues

    • 0
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Net Charge

    • 0
    • Boman Index

    • 21.89
    • Hydrophobicity

    • 1.157
    • Aliphatic Index

    • 74.29
    • Half Life

      • Mammalian:1.2 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 7240
    • Absorbance 280nm

    • 362
    • Polar Residues

    • 12

DRAMP02901

DRAMP02901 chydropathy plot
    • Function

    • Inhibits chicken myosin light chain kinase with an IC50 of 8 M. Antibacterial activity against the Gram-positive bacteria. No antibacterial activity against the Gram-negative bacteria E. coli, K. pneumoniae, P. aeruginosa, P. vulgaris, S. sonnei and S. typhosa. No antifungal activity against C. albicans.
    • Caution

    • The isopeptide linked residue 9 is shown as Asn rather than Asp as mentioned in Ref.1, because it is not known whether Asp or Asn is encoded and the isopeptide bonds are almost always formed between the amides Asn or Gln and N6-lysine or alpha amino groups, with the liberation of an ammonia that makes the reaction essentially irreversible.
    • PTM

    • Contains two disulfide bonds and D-amino acid at position 21.
  • ·Literature 1
    • Title

    • MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.--I. Isolation, structural determination and biological properties of MS-271.
    • Reference

    • Bioorg Med Chem. 1996 Jan;4(1):115-120.
    • Author

    • Yano K, Toki S, Nakanishi S, Ochiai K, Ando K, Yoshida M, Matsuda Y, Yamasaki M.