1w9n
From Proteopedia
(New page: 200px<br /><applet load="1w9n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w9n" /> '''ISOLATION AND CHARACTERIZATION OF EPILANCIN ...) |
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'''ISOLATION AND CHARACTERIZATION OF EPILANCIN 15X, A NOVEL ANTIBIOTIC FROM A CLINICAL STRAIN OF STAPHYLOCOCCUS EPIDERMIDIS'''<br /> | '''ISOLATION AND CHARACTERIZATION OF EPILANCIN 15X, A NOVEL ANTIBIOTIC FROM A CLINICAL STRAIN OF STAPHYLOCOCCUS EPIDERMIDIS'''<br /> | ||
==Overview== | ==Overview== | ||
- | The potential application of lantibiotics as food-preserving agents and | + | 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. |
==About this Structure== | ==About this Structure== | ||
- | 1W9N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http:// | + | 1W9N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Staphylococcus epidermidis]] | [[Category: Staphylococcus epidermidis]] | ||
[[Category: Ekkelenkamp, M.]] | [[Category: Ekkelenkamp, M.]] | ||
- | [[Category: Hanssen, M | + | [[Category: Hanssen, M G.M.]] |
- | [[Category: Hsu, S | + | [[Category: Hsu, S T.D.]] |
- | [[Category: Jong, A | + | [[Category: Jong, A De.]] |
[[Category: Milatovic, D.]] | [[Category: Milatovic, D.]] | ||
- | [[Category: Nuland, N | + | [[Category: Nuland, N A.J Van.]] |
[[Category: Verhoef, J.]] | [[Category: Verhoef, J.]] | ||
[[Category: lanthionine-ring]] | [[Category: lanthionine-ring]] | ||
[[Category: lantibiotic]] | [[Category: lantibiotic]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:57 2008'' |
Revision as of 13:41, 21 February 2008
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ISOLATION AND CHARACTERIZATION OF EPILANCIN 15X, A NOVEL ANTIBIOTIC FROM A CLINICAL STRAIN OF STAPHYLOCOCCUS EPIDERMIDIS
Overview
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.
About this Structure
1W9N is a Single protein structure of sequence from Staphylococcus epidermidis. Full crystallographic information is available from OCA.
Reference
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
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