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FEBS Lett ; 579(9): 1917-22, 2005 Mar 28.
Artigo em Inglês | MEDLINE | ID: mdl-15792796

RESUMO

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.


Assuntos
Antibacterianos/química , Peptídeos/química , Staphylococcus epidermidis/metabolismo , Sequência de Aminoácidos , Antibacterianos/isolamento & purificação , Bacteriocinas , Espectroscopia de Ressonância Magnética , Dados de Sequência Molecular , Peptídeos/isolamento & purificação , Processamento de Proteína Pós-Traducional , Estrutura Terciária de Proteína
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