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The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides

DOI: 10.1002/cbic.201200661 DOI Help
PMID: 23169461 PMID Help

Authors: Wael E. Houssen (University of Aberdeen) , Jesko Koehnke (University of St Andrews) , David Zollman (University of St Andrews) , Jeremie Vendome (Columbia University) , Andrea Raab (University of Aberdeen) , Margaret C. M. Smith (University of Aberdeen) , James Naismith (University of St. Andrews) , Marcel Jaspars (University of Aberdeen)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chembiochem , VOL 13 (18) , PAGES 2683 - 2689

State: Published (Approved)
Published: December 2012
Diamond Proposal Number(s): 8268

Abstract: 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.

Journal Keywords: Biosynthetic Engineering; Cyanobactins; Natural Products; Ribosomal Peptides; Subtilisin Proteases

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I03-Macromolecular Crystallography