1w9n

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Current revision (06:36, 1 May 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/LAN15_STAEP LAN15_STAEP]
[https://www.uniprot.org/uniprot/LAN15_STAEP LAN15_STAEP]
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== Publication Abstract from PubMed ==
 
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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.
 
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Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis.,Ekkelenkamp MB, Hanssen M, Danny Hsu ST, de Jong A, Milatovic D, Verhoef J, van Nuland NA FEBS Lett. 2005 Mar 28;579(9):1917-22. PMID:15792796<ref>PMID:15792796</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 1w9n" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
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Current revision

Isolation and characterization of epilancin 15X, a novel antibiotic from a clinical strain of Staphylococcus epidermidis

PDB ID 1w9n

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