Structure of PatF from Prochloron didemni

Andrew F. Bent, Jesko Koehnke, Wael E. Houssen, Margaret C. M. Smith, Marcel Jaspars, James H. Naismith*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)
2 Downloads (Pure)


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 Prochloron didemni contains a gene, patF, 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.

Original languageEnglish
Pages (from-to)618-623
Number of pages6
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Publication statusPublished - 23 May 2013


  • Macromolecular crystallography
  • Lissoclinum-patella
  • Refinement
  • Quality
  • System


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