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1.A.66.1.1
Bactericidal pore-forming pardaxin (Pa4) permeabilized both lipid and lipopolysaccharide membranes. Five paralogues are known: Pa1, 2, 3, 4, and 5, all nearly identical to each other. The 3-d structure of Pa4 is known. It forms a helix-turn-helix conformation resembling a horseshoe (Bhunia et al., 2010).

Accession Number:P81861
Protein Name:Pardaxin P-4
Length:33
Molecular Weight:3324.00
Species:Pardachirus marmoratus (Finless sole) [31087]
Location1 / Topology2 / Orientation3: Secreted1
Substrate molecule

Cross database links:

Pfam: PF07425   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0044218 C:other organism cell membrane
GO:0006811 P:ion transport
GO:0009405 P:pathogenesis

References (4)

[1] “Sequencing and synthesis of pardaxin, a polypeptide from the Red sea moses sole with ionophore activity.”  Shai Y.et.al.   2462511
[2] “Membrane composition determines pardaxin's mechanism of lipid bilayer disruption.”  Hallock K.J.et.al.   12124282
[3] “Structure and orientation of pardaxin determined by NMR experiments in model membranes.”  Porcelli F.et.al.   15292173
[4] “NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization.”  Bhunia A.et.al.   19959835
Structure:
1XC0   2KNS     

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FASTA formatted sequence 
1:	GFFALIPKII SSPLFKTLLS AVGSALSSSG GQE