| Literature DB >> 15792796 |
Miquel B Ekkelenkamp1, Micha Hanssen, Shang-Te Danny Hsu, Ad de Jong, Dana Milatovic, Jan Verhoef, Nico A J van Nuland.
Abstract
The potential application of lantibiotics as food-preserving agents and more recently as antibiotics has strongly increased the interest in these antibacterial peptides. Here, we report the elucidation of the primary and three-dimensional structures of the novel lantibiotic epilancin 15X from Staphylococcus epidermidis using high-resolution nuclear magnetic resonance spectroscopy and tandem mass spectrometry. The molecule contains ten post-translationally modified amino acids, three lanthionine ring structures and a hydroxy-propionyl N-terminal moiety. The primary and tertiary structure and the distribution of positive charges are closely similar to the previously identified lantibiotic epilancin K7, most likely indicative of a common mode of action.Entities:
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Year: 2005 PMID: 15792796 DOI: 10.1016/j.febslet.2005.01.083
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124