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Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE 1–34
Author(s) -
Houssen Wael E.,
Wright Stephen H.,
Kalverda Arnout P.,
Thompson Gary S.,
Kelly Sharon M.,
Jaspars Marcel
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000305
Subject(s) - sequence (biology) , peptide , peptide sequence , helix (gastropod) , chemistry , stereochemistry , molecular dynamics , crystallography , biochemistry , biology , computational chemistry , gene , ecology , snail
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.