title: 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 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.
authors.affiliation: Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign , 600 South Mathews Avenue, Urbana, Illinois 61801, United States.
authors.forename: Chantal V
authors.initials: CV
authors.lastname: Garcia De Gonzalo
authors.forename: Lingyang
authors.initials: L
authors.lastname: Zhu
authors.forename: Trent J
authors.initials: TJ
authors.lastname: Oman
authors.forename: Wilfred A
authors.initials: WA
authors.lastname: van der Donk
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism*; D001430:Bacteriocins / Q000737:chemistry* / Q000302:isolation & purification; D006020:Glycopeptides / Q000737:chemistry* / Q000302:isolation & purification; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D001430:Bacteriocins; D006020:Glycopeptides; C114602:sublancin 168