2A2B

Curvacin A

Summary for 2A2B

• Entry DOI: 10.2210/pdb2a2b/pdb
• NMR Information: BMRB: 6737
• Descriptor: Bacteriocin curvacin A (1 entity in total)
• Functional Keywords: alfa helix, beta-sheet like strukture, antibiotic
• Biological source: Lactobacillus curvatus
• Cellular location: Secreted: P0A311
• Total number of polymer chains: 1
• Total formula weight: 4312.89

Authors

Haugen, H.S.,Kristiansen, P.E. (deposition date: 2005-06-22, release date: 2006-06-13, Last modification date: 2024-11-20)

Primary citation

Haugen, H.S.,Fimland, G.,Nissen-Meyer, J.,Kristiansen, P.E.
Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A
Biochemistry, 44:16149-16157, 2005

PubMed Abstract: The 3D structure of the membrane-permeabilizing 41-mer pediocin-like antimicrobial peptide curvacin A produced by lactic acid bacteria has been studied by NMR spectroscopy. In DPC micelles, the cationic and hydrophilic N-terminal half of the peptide forms an S-shaped beta-sheet-like domain stabilized by a disulfide bridge and a few hydrogen bonds. This domain is followed by two alpha-helices: a hydrophilic 6-mer helix between residues 19 and 24 and an amphiphilic/hydrophobic 11-mer helix between residues 29 and 39. There are two hinges in the peptide, one at residues 16-18 between the N-terminal S-shaped beta-sheet-like structure and the central 6-mer helix and one at residues 26-28 between the central helix and the 11-mer C-terminal helix. The latter helix is the only amphiphilic/hydrophobic part of the peptide and is thus presumably the part that penetrates into the hydrophobic phase of target-cell membranes. The hinge between the two helices may introduce the flexibility that allows the helix to dip into membranes. The helix-hinge-helix structure in the C-terminal half of curvacin A clearly distinguishes this peptide from the other pediocin-like peptides whose structures have been analyzed and suggests that curvacin A along with the structural homologues enterocin P and carnobacteriocin BM1 belong to a subgroup of the pediocin-like family of antimicrobial peptides.

PubMed: 16331975
DOI: 10.1021/bi051215u

Experimental method

SOLUTION NMR