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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 6(69), p. 618-623, 2013

DOI: 10.1107/s1744309113012931

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Structure of PatF fromProchloron didemni

Journal article published in 2013 by Andrew F. Bent, Jesko Koehnke, Wael E. Houssen ORCID, Margaret C. M. Smith, Marcel Jaspars, James H. Naismith ORCID
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.