1OHN

Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P.

Summary for 1OHN

• Entry DOI: 10.2210/pdb1ohn/pdb
• Related: 1OG7 1OHM
• Descriptor: BACTERIOCIN SAKACIN P (1 entity in total)
• Functional Keywords: antibiotic, pediocin-like bacteriocins, antimicrobial peptides, sakacin antibiotic, bacteriocin
• Biological source: LACTOBACILLUS SAKE
• Cellular location: Secreted: P35618
• Total number of polymer chains: 1
• Total formula weight: 4441.82

Authors

Uteng, M.,Hauge, H.H.,Markwick, P.R.,Fimland, G.,Mantzilas, D.,Nissen-Meyer, J.,Muhle-Goll, C. (deposition date: 2003-05-28, release date: 2003-09-22, Last modification date: 2024-10-09)

Primary citation

Uteng, M.,Hauge, H.H.,Markwick, P.R.,Fimland, G.,Mantzilas, D.,Nissen-Meyer, J.,Muhle-Goll, C.
Three-Dimensional Structure in Lipid Micelles of the Pediocin-Like Antimicrobial Peptide Sakacin P and a Sakacin P Variant that is Structurally Stabilized by an Inserted C-Terminal Disulfide Bridge
Biochemistry, 42:11417-, 2003

PubMed Abstract: The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacin P (termed sakP[N24C+44C]) have been determined by use of nuclear magnetic resonance spectroscopy. SakP[N24C+44C] has an inserted non-native activity- and structure-stabilizing C-terminal disulfide bridge that ties the C-terminus to the middle part of the peptide. In the presence of DPC, the cationic N-terminal region (residues 1-17) of both peptides has an S-shaped conformation that is reminiscent of a three-stranded antiparallel beta-sheet and that is more pronounced when the peptide was dissolved in TFE instead of DPC. The four positively charged residues located in the N-terminal part are found pointing to the same direction. For both peptides, the N-terminal region is followed by a well-defined central amphiphilic alpha-helix (residues 18-33), and this in turn is followed by the C-terminal tail (residues 34-43 for sakacin P and 34-44 for sakP[N24C+44C]) that lacks any apparent common secondary structural motif. In the presence of DPC, the C-terminal tails in both peptides fold back onto the central alpha-helix, thereby creating a hairpin-like structure in the C-terminal halves. The lack of long-range NOEs between the beta-sheet Nu-terminal region and the hairpin-like C-terminal half indicates that there is a flexible hinge between these regions. We discuss which implications such a structural arrangement has on the interaction with the target cell membrane.

PubMed: 14516192
DOI: 10.1021/BI034572I

Experimental method

SOLUTION NMR