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

Wael E Houssen , Stephen Henry Wright, Arnout P. Kalverda, Gary S. Thompson, Sharon M. Kelly, Marcel Jaspars

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


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 a-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.

Original languageEnglish
Pages (from-to)1867-1873
Number of pages7
Issue number13
Early online date16 Aug 2010
Publication statusPublished - 3 Sept 2010


  • biosynthesis
  • cyanobactins
  • patellamides
  • peptides
  • Prochloron
  • protein secondary structure
  • 2-dimensional NMR-spectroscopy
  • carboxylation recognition site
  • microcin B17
  • mutational analysis
  • lissoclinum-patella
  • escherichia-coli
  • natural-product
  • gene-cluster


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