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Biochemistry. 2011 Apr 12;50(14):2748-55. doi: 10.1021/bi200217u. Epub 2011 Mar 21.

Structural, dynamic, and chemical characterization of a novel S-glycosylated bacteriocin.

Author information

1
Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand. h.venugopal@massey.ac.nz

Abstract

Bacteriocins are bacterial peptides with specific activity against competing species. They hold great potential as natural preservatives and for their probiotic effects. We show here nuclear magnetic resonance-based evidence that glycocin F, a 43-amino acid bacteriocin from Lactobacillus plantarum, contains two β-linked N-acetylglucosamine moieties, attached via side chain linkages to a serine via oxygen, and to a cysteine via sulfur. The latter linkage is novel and has helped to establish a new type of post-translational modification, the S-linked sugar. The peptide conformation consists primarily of two α-helices held together by a pair of nested disulfide bonds. The serine-linked sugar is positioned on a short loop sequentially connecting the two helices, while the cysteine-linked sugar presents at the end of a long disordered C-terminal tail. The differing chemical and conformational stabilities of the two N-actetylglucosamine moieties provide clues about the possible mode of action of this bacteriostatic peptide.

PMID:
21395300
DOI:
10.1021/bi200217u
[Indexed for MEDLINE]

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