NMR structure of the S-linked glycopeptide sublancin 168

Chantal V. Garcia De Gonzalo, Lingyang Zhu, Trent J. Oman, Wilfred A. Van Der Donk

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)796-801
Number of pages6
JournalACS chemical biology
Issue number3
StatePublished - Mar 21 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine


Dive into the research topics of 'NMR structure of the S-linked glycopeptide sublancin 168'. Together they form a unique fingerprint.

Cite this