NMR structure of the S-linked glycopeptide sublancin 168

ACS Chem Biol. 2014 Mar 21;9(3):796-801. doi: 10.1021/cb4008106. Epub 2014 Jan 17.

Abstract

Sublancin 168 is a member of a small group of glycosylated antimicrobial peptides known as glycocins. The solution structure of sublancin 168, a 37-amino-acid peptide produced by Bacillus subtilis 168, has been solved by nuclear magnetic resonance (NMR) spectroscopy. Sublancin comprises two α-helices and a well-defined interhelical loop. The two helices span residues 6-16 and 26-35, and the loop region encompasses residues 17-25. The 9-amino-acid loop region contains a β-S-linked glucose moiety attached to Cys22. Hydrophobic interactions as well as hydrogen bonding are responsible for the well-structured loop region. The three-dimensional structure provides an explanation for the previously reported extraordinary high stability of sublancin 168.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacillus subtilis / metabolism*
  • Bacteriocins / chemistry*
  • Bacteriocins / isolation & purification
  • Glycopeptides / chemistry*
  • Glycopeptides / isolation & purification
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Magnetic Resonance Spectroscopy
  • Protein Stability
  • Protein Structure, Secondary

Substances

  • Bacteriocins
  • Glycopeptides
  • sublancin 168