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NMR structure of the S-linked glycopeptide sublancin 168.

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 ?-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 ?-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.

SUBMITTER: Garcia De Gonzalo CV

PROVIDER: S-EPMC3985867 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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NMR structure of the S-linked glycopeptide sublancin 168.

Garcia De Gonzalo Chantal V CV Zhu Lingyang L Oman Trent J TJ van der Donk Wilfred A WA

ACS chemical biology 20140117 3

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 ...[more]

PMID: 24405370

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