Structural highlights
Function
SUNA_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 PubMed
Sublancin 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
- ↑ Oman TJ, Boettcher JM, Wang H, Okalibe XN, van der Donk WA. Sublancin is not a lantibiotic but an S-linked glycopeptide. Nat Chem Biol. 2011 Feb;7(2):78-80. doi: 10.1038/nchembio.509. Epub 2011 Jan 2. PMID:21196935 doi:http://dx.doi.org/10.1038/nchembio.509
- ↑ Garcia De Gonzalo CV, Zhu L, Oman TJ, van der Donk WA. NMR Structure of the S-Linked Glycopeptide Sublancin 168. ACS Chem Biol. 2014 Jan 17. PMID:24405370 doi:http://dx.doi.org/10.1021/cb4008106
