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

• Published in: Chembiochem : a European journal of chemical biology Vol. 11; no. 13; pp. 1867 - 1873
• Main Authors: Houssen , Wael E., Wright, Stephen H., Kalverda, Arnout P., Thompson, Gary S., Kelly, Sharon M., Jaspars, Marcel
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 03.09.2010; WILEY‐VCH Verlag
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; biosynthesis; Circular Dichroism; cyanobactins; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Molecular Dynamics Simulation; Molecular Sequence Data; patellamides; peptides; Peptides - chemistry; Prochloron; Prochloron - enzymology; Protein Precursors - chemistry; Protein Sorting Signals; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.201000305

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. 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.