Structure of PatF from Prochloron didemni. Issue 6 (31st May 2013)

• Record Type: Journal Article
• Authors: Bent, Andrew F.; Koehnke, Jesko; Houssen, Wael E.; Smith, Margaret C. M.; Jaspars, Marcel; Naismith, James H.
• Is Part Of: Acta crystallographica. Volume 69:Issue 6(2013:Jun.)
• Page Start: 618
• Page End: 623
• Publication Date: 2013-05-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113012931
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Patellamides are macrocyclic peptides with potent biological effects and are a subset of the cyanobactins. Cyanobactins are natural products that are produced by a series of enzymatic transformations and a common modification is the addition of a prenyl group. Puzzlingly, the pathway for patellamides in <italic>Prochloron didemni</italic> contains a gene, <italic>patF</italic>, with homology to prenylases, but patellamides are not themselves prenylated. The structure of the protein PatF was cloned, expressed, purified and determined. Prenylase activity could not be demonstrated for the protein, and examination of the structure revealed changes in side‐chain identity at the active site. It is suggested that these changes have inactivated the protein. Attempts to mutate these residues led to unfolded protein.</p> </abstract>