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The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides
Author(s) -
Houssen Wael E.,
Koehnke Jesko,
Zollman David,
Vendome Jeremie,
Raab Andrea,
Smith Margaret C. M.,
Naismith James H.,
Jaspars Marcel
Publication year - 2012
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.201200661
Subject(s) - serine protease , biochemistry , protease , aquifex aeolicus , enzyme , biology , ribosomal rna , computational biology , chemistry , escherichia coli , gene
Cyanobactins, including patellamides, are a group of cyanobacterial post‐translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin‐like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds.