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Structure of PatF from Prochloron didemni
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 patellamide...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668578/ https://www.ncbi.nlm.nih.gov/pubmed/23722837 http://dx.doi.org/10.1107/S1744309113012931 |
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author | Bent, Andrew F. Koehnke, Jesko Houssen, Wael E. Smith, Margaret C. M. Jaspars, Marcel Naismith, James H. |
author_facet | Bent, Andrew F. Koehnke, Jesko Houssen, Wael E. Smith, Margaret C. M. Jaspars, Marcel Naismith, James H. |
author_sort | Bent, Andrew F. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3668578 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-36685782013-06-04 Structure of PatF from Prochloron didemni Bent, Andrew F. Koehnke, Jesko Houssen, Wael E. Smith, Margaret C. M. Jaspars, Marcel Naismith, James H. Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications 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. International Union of Crystallography 2013-05-23 /pmc/articles/PMC3668578/ /pubmed/23722837 http://dx.doi.org/10.1107/S1744309113012931 Text en © Bent et al. 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Structural Communications Bent, Andrew F. Koehnke, Jesko Houssen, Wael E. Smith, Margaret C. M. Jaspars, Marcel Naismith, James H. Structure of PatF from Prochloron didemni |
title | Structure of PatF from Prochloron didemni
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title_full | Structure of PatF from Prochloron didemni
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title_fullStr | Structure of PatF from Prochloron didemni
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title_full_unstemmed | Structure of PatF from Prochloron didemni
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title_short | Structure of PatF from Prochloron didemni
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title_sort | structure of patf from prochloron didemni |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668578/ https://www.ncbi.nlm.nih.gov/pubmed/23722837 http://dx.doi.org/10.1107/S1744309113012931 |
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