2mij
From Proteopedia
NMR structure of the S-linked glycopeptide sublancin 168
Structural highlights
FunctionSUNA_BACSU Bacteriocin active against Gram-positive bacteria. Inhibits B.cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells. Inhibits B.subtilis strain ATCC 6633.[1] Publication Abstract from PubMedSublancin 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 alpha-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 beta-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. NMR Structure of the S-Linked Glycopeptide Sublancin 168.,Garcia De Gonzalo CV, Zhu L, Oman TJ, van der Donk WA ACS Chem Biol. 2014 Jan 17. PMID:24405370[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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