Volume 11, Issue 13 p. 1867-1873
Full Paper

Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1–34

Wael E. Houssen  Dr.

Wael E. Houssen  Dr.

Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Aberdeen AB24 3UE, Scotland (UK), Fax: (+44) 1224-272921

These authors contributed equally to this work.

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Stephen H. Wright Dr.

Stephen H. Wright Dr.

Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Aberdeen AB24 3UE, Scotland (UK), Fax: (+44) 1224-272921

These authors contributed equally to this work.

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Arnout P. Kalverda Dr.

Arnout P. Kalverda Dr.

Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT (UK)

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Gary S. Thompson Dr.

Gary S. Thompson Dr.

Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT (UK)

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Sharon M. Kelly Dr.

Sharon M. Kelly Dr.

Division of Molecular and Cellular Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow GI2 8QQ (UK)

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Marcel Jaspars Prof.

Marcel Jaspars Prof.

Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Aberdeen AB24 3UE, Scotland (UK), Fax: (+44) 1224-272921

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First published: 16 August 2010
Citations: 21

Graphical Abstract

Follow the helical leader: The solution structure of the leader sequence of the patellamide precursor peptide, which is assumed to target it to the post-translational machinery has been studied. This sequence was observed to form an α-helix spanning residues 13–28 with a hydrophobic surface on one side of the helix. This surface is proposed to be the site of the initial binding with modifying enzymes.

Abstract

The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an α-helix spanning residues 13–28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.