General Information

    • DRAMP ID

    • DRAMP03320

    • Peptide Name

    • Pore-forming peptide ameobapore A (EH-APP; saposin-like protein)

    • Source

    • Entamoeba histolytica (protozoan parasite)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GEILCNLCTGLINTLENLLTTKGADKVKDYISSLCNKASGFIATLCTKVLDFGIDKLIQLIEDKVDANAICAKIHAC

    • Sequence Length

    • 77

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

      • Gram-positive bacteria: Micrococcus luteus (MIC=1.9 µM), Bacillus megaterium (MIC=13 µM), Bacillus subtilis (MIC=27 µM), Staphylococcus aureus (MIC>15 µM).

    • 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

    • Cell membrane

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Cyclization(Cys5 and Cys77).

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bonds between Cys5 and Cys77,Cys8 and Cys71,Cys35 and Cys46.

    • Stereochemistry

    • L

    • Structure

    • Alpha helix (5 helices; 53 residues)

    • Structure Description

    • Amoebapore A belongs to the superfamily of saposin-like proteins that are characterized by a conserved disulfide bond pattern and a fold consisting of five helices.(Ref.3)

    • Helical Wheel Diagram

    • DRAMP03320 helical wheel diagram

    • PDB ID

    • 1OF9 resolved by NMR.
  • 1OF9-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP03320.

Physicochemical Information

    • Formula

    • C362H605N93O112S6

    • Absent Amino Acids

    • MPRW

    • Common Amino Acids

    • L

    • Mass

    • 8244.7

    • PI

    • 5.65

    • Basic Residues

    • 9

    • Acidic Residues

    • 9

    • Hydrophobic Residues

    • 32

    • Net Charge

    • 0

    • Boman Index

    • -44.78

    • Hydrophobicity

    • 0.407

    • Aliphatic Index

    • 121.69

    • Half Life

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

    • Extinction Coefficient Cystines

    • 1865

    • Absorbance 280nm

    • 24.54

    • Polar Residues

    • 26

DRAMP03320

DRAMP03320 chydropathy plot

Comments Information

    • Forms pores in the cytoplasmic membrane of host cells. Implicated in the cytolytic activity of the parasite.

Literature Information

  • ·Literature 1

    • Title

    • Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes.

    • Reference

    • Mol Microbiol. 1994 Dec;14(5):895-904.

    • Author

    • Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ.
  • ·Literature 2

    • Title

    • Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.

    • Reference

    • Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2602-2606.

    • Author

    • Leippe M, Andrä J, Müller-Eberhard HJ.
  • ·Literature 3

    • Title

    • Solution structure of the pore-forming protein of Entamoeba histolytica.

    • Reference

    • J Biol Chem. 2004 Apr 23;279(17):17834-41.

    • Author

    • Hecht O, Van Nuland NA, Schleinkofer K, Dingley AJ, Bruhn H, Leippe M, Grötzinger J.