Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34.
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 alpha-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.
Houssen
Wael E
WE
Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Aberdeen AB24 3UE, Scotland, UK.
Wright
Stephen H
SH
Kalverda
Arnout P
AP
Thompson
Gary S
GS
Kelly
Sharon M
SM
Jaspars
Marcel
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D019691:Prochloron / Q000201:enzymology; D011498:Protein Precursors / Q000737:chemistry*; D021382:Protein Sorting Signals; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D010455:Peptides; D011498:Protein Precursors; D021382:Protein Sorting Signals