Cyclic lipoundecapeptide amphisin from Pseudomonas sp. strain DSS73 |
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Authors: | Dan Srensen Tommy H Nielsen Carsten Christophersen Jan Srensen Michael Gajhede |
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Institution: | Dan Sørensen,Tommy H. Nielsen,Carsten Christophersen,Jan Sørensen,Michael Gajhede |
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Abstract: | The crystal structure of the lipoundecapeptide amphisin, presented here as the tetrahydrate, C66H114N12O20·4H2O, originating from non‐ribosomal biosynthesis by Pseudomonas sp. strain DSS73, has been solved to a resolution of 0.65 Å. The primary structure of amphisin is β‐hydroxydecanoyl‐d ‐Leu‐d ‐Asp‐d ‐allo‐Thr‐d ‐Leu‐d ‐Leu‐d ‐Ser‐l ‐Leu‐d ‐Gln‐l ‐Leu‐l ‐Ile‐l ‐Asp (Leu is leucine, Asp is aspartic acid, Thr is threonine, Ser is serine, Gln is glutamine and Ile is isoleucine). The peptide is a lactone, linking Thr4 Oγ to the C‐terminal. The stereochemistry of the β‐hydroxy acid is R. The peptide is a close analogue of the cyclic lipopeptides tensin and pholipeptin produced by Pseudomonas fluorescens. The structure of amphisin is mainly helical (310‐helix), with the cyclic peptide wrapping around a hydrogen‐bonded water molecule. This lipopeptide is amphiphilic and has biosurfactant and antifungal properties. |
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