Title | Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis. |
Publication Type | Journal Article |
Year of Publication | 2005 |
Authors | Ekkelenkamp, M. B., M. Hanssen, S-T. D. Hsu, A. de Jong, D. Milatovic, J. Verhoef, and N. A. J. van Nuland |
Journal | FEBS Lett |
Volume | 579 |
Issue | 9 |
Pagination | 1917-22 |
Date Published | 2005 Mar 28 |
ISSN | 0014-5793 |
Keywords | Amino Acid Sequence, Anti-Bacterial Agents, Bacteriocins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptides, Protein Processing, Post-Translational, Protein Structure, Tertiary, Staphylococcus epidermidis |
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. |
DOI | 10.1016/j.febslet.2005.01.083 |
Alternate Journal | FEBS Lett. |
PubMed ID | 15792796 |
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