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.
Original language | English (US) |
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Pages (from-to) | 796-801 |
Number of pages | 6 |
Journal | ACS chemical biology |
Volume | 9 |
Issue number | 3 |
DOIs | |
State | Published - Mar 21 2014 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine