General Information

    • 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

    • SMILES

    • Not available

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal

    • Target Organism

    • Target OrganismActivity
      Alternaria helianthiMIC=2-5 µg/ml
      Botrytis cinereaMIC=5-10 µg/ml
      Ceratocystis parodoxaMIC=20 µg/ml
      Colletotrichum gloeosporioidesMIC=2-5 µg/ml
      Fusurium oxysporumMIC=2-5 µg/ml
      Leptosphaeria maculansMIC=5 µg/ml
      Macrophomina phaseolinaMIC<25 µg/ml
      Phytophthoru cryptogeaMIC=5-10 µg/ml
      Pythium graminicolaMIC=5 µg/ml
      Sclerotinia sclerotiorum sporesMIC=5 µg/ml
      Sclerotinia sclerotiorum myceliaMIC=50 µg/ml
      Verticilium dahliaeMIC=2 µg/ml
      Clavibacter michiganensisMIC<10 µg/ml
      Saccharomyces cerevisiaeMIC=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

Structure Information

    • 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)

    • PDB ID

    • 1C01 resolved by NMR.

    • Predicted Structure

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.