Structural highlights
Function
Q52QI9_PRODI
Publication Abstract from PubMed
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.
The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides.,Houssen WE, Koehnke J, Zollman D, Vendome J, Raab A, Smith MC, Naismith JH, Jaspars M Chembiochem. 2012 Nov 21. doi: 10.1002/cbic.201200661. PMID:23169461[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Houssen WE, Koehnke J, Zollman D, Vendome J, Raab A, Smith MC, Naismith JH, Jaspars M. The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides. Chembiochem. 2012 Nov 21. doi: 10.1002/cbic.201200661. PMID:23169461 doi:http://dx.doi.org/10.1002/cbic.201200661