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

TY - JOUR

T1 - Structural, dynamic, and chemical characterization of a novel S-glycosylated bacteriocin

AU - Venugopal, Hariprasad

AU - Edwards, Patrick J B

AU - Schwalbe, Martin

AU - Claridge, Jolyon K

AU - Libich, David S

AU - Stepper, Judith

AU - Loo, Trevor

AU - Patchett, Mark L

AU - Norris, Gillian E

AU - Pascal, Steven M

PY - 2011/4/12

Y1 - 2011/4/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=79953711158&partnerID=8YFLogxK

U2 - 10.1021/bi200217u

DO - 10.1021/bi200217u

M3 - Article

C2 - 21395300

SN - 1520-4995

VL - 50

SP - 2748

EP - 2755

JO - Biochemistry

JF - Biochemistry

IS - 14

ER -