• DRAMP ID

    • DRAMP00933
    • Peptide Name

    • Antimicrobial peptide 1 (AMP1; MiAMP1; Plant defensin)
    • Source

    • Macadamia integrifolia (Macadamia nut)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • SAFTVWSGPGCNNRAERYSKCGCSAIHQKGGYDFSYTGQTAALYNQAGCSGVAHTRFGSSARACNPFGWKSIFIQC
    • Sequence Length

    • 76
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal
    • Target Organism

    • Alternaria helianthi (MIC=2-5 µg/ml), Botrytis cinerea (MIC=5-10 µg/ml), Ceratocystis parodoxa (MIC=20 µg/ml), Colletotrichum gloeosporioides (MIC=2-5 µg/ml), Fusurium oxysporum (MIC=2-5 µg/ml), Leptosphaeria maculans (MIC=5 µg/ml), Macrophomina phaseolina (MIC<25 µg/ml), Phytophthoru cryptogea (MIC=5-10 µg/ml), Pythium graminicola (MIC=5 µg/ml), Sclerotinia sclerotiorum spores (MIC=5 µg/ml), Sclerotinia sclerotiorum mycelia (MIC=50 µg/ml), Verticilium dahliae (MIC=2 µg/ml), Clavibacter michiganensis (MIC<10 µg/ml), Saccharomyces cerevisiae (MIC=2-5 µg/ml).
    • Hemolytic Activity

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

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Cyclization of a C-terminal Cys residue (forming a disulfide bond)
    • Nonterminal Modifications and Unusual Amino Acids

    • [Ref.10543955] There are three disulfide bonds between Cys11 and Cys64, Cys21 and Cys76, Cys23 and Cys49
    • Stereochemistry

    • L
    • Structure

    • Combine helix and strand structure
    • Structure Description

    • MiAMP1 is made up of eight beta-strands which are arranged in two Greek key motifs. These Greek key motifs associate to form a Greek key beta-barrel. This structure is unique amongst plant antimicrobial proteins and forms a new class which we term the beta-barrelins. (Ref.2)
    • Helical Wheel Diagram

    • DRAMP00933 helical wheel diagram
    • PDB ID

    • 1C01 resolved by NMR.
    • Predicted Structure

    • There is no predicted structure for DRAMP00933.
    • Formula

    • C354H523N105O106S6
    • Absent Amino Acids

    • M
    • Common Amino Acids

    • GAS
    • Mass

    • 8138.05
    • PI

    • 9.08
    • Basic Residues

    • 9
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 22
    • Net Charge

    • +7
    • Boman Index

    • -110.65
    • Hydrophobicity

    • -0.321
    • Aliphatic Index

    • 40
    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 17335
    • Absorbance 280nm

    • 231.13
    • Polar Residues

    • 37

DRAMP00933

DRAMP00933 chydropathy plot
    • Function

    • Antimicrobial peptide which inhibits the growth of a variety of fungi, oomycetes, Gram-positive bacterial phytopatogenes and S.cerevisiae in vitro. No activity against E.coli.
    • Miscellaneous

    • Its antimicrobial activity is diminished by calcium an
  • ·Literature 1
    • Title

    • Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia.
    • Reference

    • Eur J Biochem. 1997 Mar 15;244(3):743-749.
    • Author

    • Marcus JP, Goulter KC, Green JL, Harrison SJ, Manners JM.
  • ·Literature 2
    • Title

    • MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins.
    • Reference

    • J Mol Biol. 1999 Oct 29;293(3):629-638.
    • Author

    • McManus AM, Nielsen KJ, Marcus JP, Harrison SJ, Green JL, Manners JM, Craik DJ.