Structural, dynamic, and chemical characterization of a novel S-glycosylated bacteriocin.
Biochemistry, 2011/4/12;50(14):2748-55.
Venugopal H[1], Edwards PJ, Schwalbe M, Claridge JK, Libich DS, Stepper J, Loo T, Patchett ML, Norris GE, Pascal SM
Affiliations
PMID: 21395300DOI: 10.1021/bi200217u
Impact factor: 3.321
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.
MeSH terms
Acetylglucosamine; Bacteriocins; Cysteine; Disulfides; Glycosylation; Kinetics; Lactobacillus plantarum; Magnetic Resonance Spectroscopy; Models, Molecular; Oxygen; Protein Conformation; Protein Processing, Post-Translational; Protein Structure, Secondary; Serine; Sulfur
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