2KUY

Structure of Glycocin F

Summary for 2KUY

• Entry DOI: 10.2210/pdb2kuy/pdb
• NMR Information: BMRB: 16747
• Descriptor: Prebacteriocin glycocin F, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: bacteriocin, glycosylation, lactobacillus, s-linked, antimicrobial protein
• Biological source: Lactobacillus plantarum
• Total number of polymer chains: 1
• Total formula weight: 5248.80

Authors

Venugopal, H.,Edwards, P.,Schwalbe, M.,Claridge, J.,Stepper, J.,Patchett, M.,Loo, T.,Libich, D.,Norris, G.,Pascal, S. (deposition date: 2010-03-01, release date: 2011-05-04, Last modification date: 2024-11-20)

Primary citation

Venugopal, H.,Edwards, P.J.,Schwalbe, M.,Claridge, J.K.,Libich, D.S.,Stepper, J.,Loo, T.,Patchett, M.L.,Norris, G.E.,Pascal, S.M.
Structural, dynamic, and chemical characterization of a novel s-glycosylated bacteriocin.
Biochemistry, 50:2748-2755, 2011

PubMed 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.

PubMed: 21395300
DOI: 10.1021/bi200217u

Experimental method

SOLUTION NMR