• DRAMP ID

    • DRAMP00856
    • Peptide Name

    • Kalata-B1 (Plant defensin)
    • Source

    • Oldenlandia affinis
    • Family

    • Belongs to the cyclotide family
    • Gene

    • OAK1
    • Sequence

    • GLPVCGETCVGGTCNTPGCTCSWPVCTRN
    • Sequence Length

    • 29
    • Evidence code

    • Protein level
    • Biological Activity

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

      • [Ref.10430870]Gram-positive bacterium: Staphylococcus aureus (MIC=0.26 µM), Micrococcus luteus (MIC=40.4 µM);
      • Gram-negative bacterium: Klebsiella oxytoca (MIC=54.8 µM);
      • Fungi: Candida kefyr (MIC=21.4 µM).
    • Hemolytic activity

      • [Ref:17534989]20% hemolytic activity at 0.6μM and 75% hemolytic activity at 1.5μM against human type A red blood cells
    • Binding Target

    • Cell membrance
    • Structure

    • Beta strand (3 strands; 7 residues)
    • Structure Description

    • Unknown
    • PDB ID

    • 2KHB resolved by NMR.
    • DRAMP00856 helical wheel diagram
    • 2KHB-> 
    • Formula

    • C117H187N35O40S6
    • Absent Amino Acids

    • ADFHIKMQY
    • Common Amino Acids

    • C
    • Mass

    • 3415.96
    • PI

    • 5.94
    • Basic Residues

    • 1
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 5
    • Boman Index

    • -19.51
    • Hydrophobicity

    • 15.17
    • Aliphatic Index

    • 43.45
    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5875
    • Absorbance 280nm

    • 209.82
    • Polar Residues

    • 19

DRAMP00856

DRAMP00856 chydropathy plot
    • Function

    • Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S. aureus. Relatively ineffective against Gram-negative bacteria such as E. coli and P. aeruginosa. Inhibitory effect on the growth and development of larvae from H. punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost.
    • MOA

    • a small number of cyclotides bind to the membrane surface and then insert first into the outer membrane leaflet followed by penetration through the membrane and pore formation. At higher concentrations of cyclotides, destabilization of membranes occurs.
    • Tissue specificity

    • Leaves and stems. Lower in roots.
    • Pharmaceutical use

    • The uteroactive properties of Kalata have been discovered by African traditional medicine. It is used as an ingredient of a herbal tea to accelerate childbirth.
    • PTM

    • Kalata-B1 is a cyclic peptide which contains three disulfide bonds 5-19; 11-21; 14-26.
  • Literature 1
    • Reference

    • Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8918.
    • Author

    • Tam JP, Lu YA, Yang JL, Chiu KW.
    • Title

    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.
  • Literature 2
    • Reference

    • Biochemistry. 1995 Apr 4;34(13):4147-4158.
    • Author

    • Saether O, Craik DJ, Campbell ID, Sletten K, Juul J, Norman DG.
    • Title

    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1.
  • Literature 3
    • Reference

    • Chembiochem. 2007 Jun 18;8(9):1001-1011.
    • Author

    • Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.
    • Title

    • The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.
  • Literature 4
    • Reference

    • Biochemistry. 2003 Jun 10;42(22):6688-6695.
    • Author

    • Barry DG, Daly NL, Clark RJ, Sando L, Craik DJ.
    • Title

    • Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity.
  • Literature 5
    • Reference

    • J Biol Chem. 2012 Dec
    • Author

    • Wang CK, Wacklin HP, Craik DJ.
    • Title

    • Cyclotides insert into lipid bilayers to for