Structure of PatF from Prochloron didemni

Bent, A. F., Koehnke, J. , Houssen, W. E., Smith, M. C.M., Jaspars, M. and Naismith, J. H. (2013) Structure of PatF from Prochloron didemni. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 69, pp. 618-623. (doi: 10.1107/S1744309113012931) (PMID:23722837) (PMCID:PMC3668578)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Koehnke, Dr Jesko
Authors: Bent, A. F., Koehnke, J., Houssen, W. E., Smith, M. C.M., Jaspars, M., and Naismith, J. H.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Publisher:International Union of Crystallography
ISSN:1744-3091
ISSN (Online):2053-230X
Copyright Holders:Copyright © 2013 The Authors
First Published:First published in Acta Crystallographica. Section F: Structural Biology Communications F69: 618–623
Publisher Policy:Reproduced under a Creative Commons licence

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