Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.

Bacterial microcompartments form a protective proteinaceous barrier around metabolic enzymes that process unstable or toxic chemical intermediates. The genome of the virulent, multidrug-resistant Clostridium difficile 630 strain contains an operon, eut, encoding a bacterial microcompartment with gen...

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Autores principales:	Alison C Pitts, Laura R Tuck, Alexandra Faulds-Pain, Richard J Lewis, Jon Marles-Wright
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/49b1a2d466264d819020a2ff84b62008
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spelling	oai:doaj.org-article:49b1a2d466264d819020a2ff84b620082021-11-18T08:10:43ZStructural insight into the Clostridium difficile ethanolamine utilisation microcompartment.1932-620310.1371/journal.pone.0048360https://doaj.org/article/49b1a2d466264d819020a2ff84b620082012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23144756/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Bacterial microcompartments form a protective proteinaceous barrier around metabolic enzymes that process unstable or toxic chemical intermediates. The genome of the virulent, multidrug-resistant Clostridium difficile 630 strain contains an operon, eut, encoding a bacterial microcompartment with genes for the breakdown of ethanolamine and its utilisation as a source of reduced nitrogen and carbon. The C. difficile eut operon displays regulatory genetic elements and protein encoding regions in common with homologous loci found in the genomes of other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. The crystal structures of two microcompartment shell proteins, CD1908 and CD1918, and an uncharacterised protein with potential enzymatic activity, CD1925, were determined by X-ray crystallography. CD1908 and CD1918 display the same protein fold, though the order of secondary structure elements is permuted in CD1908 and this protein displays an N-terminal β-strand extension. These proteins form hexamers with molecules related by crystallographic and non-crystallographic symmetry. The structure of CD1925 has a cupin β-barrel fold and a putative active site that is distinct from the metal-ion dependent catalytic cupins. Thin-section transmission electron microscopy of Escherichia coli over-expressing eut proteins indicates that CD1918 is capable of self-association into arrays, suggesting an organisational role for CD1918 in the formation of this microcompartment. The work presented provides the basis for further study of the architecture and function of the C. difficile eut microcompartment, its role in metabolism and the wider consequences of intestinal colonisation and virulence in this pathogen.Alison C PittsLaura R TuckAlexandra Faulds-PainRichard J LewisJon Marles-WrightPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e48360 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alison C Pitts Laura R Tuck Alexandra Faulds-Pain Richard J Lewis Jon Marles-Wright Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.
description	Bacterial microcompartments form a protective proteinaceous barrier around metabolic enzymes that process unstable or toxic chemical intermediates. The genome of the virulent, multidrug-resistant Clostridium difficile 630 strain contains an operon, eut, encoding a bacterial microcompartment with genes for the breakdown of ethanolamine and its utilisation as a source of reduced nitrogen and carbon. The C. difficile eut operon displays regulatory genetic elements and protein encoding regions in common with homologous loci found in the genomes of other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. The crystal structures of two microcompartment shell proteins, CD1908 and CD1918, and an uncharacterised protein with potential enzymatic activity, CD1925, were determined by X-ray crystallography. CD1908 and CD1918 display the same protein fold, though the order of secondary structure elements is permuted in CD1908 and this protein displays an N-terminal β-strand extension. These proteins form hexamers with molecules related by crystallographic and non-crystallographic symmetry. The structure of CD1925 has a cupin β-barrel fold and a putative active site that is distinct from the metal-ion dependent catalytic cupins. Thin-section transmission electron microscopy of Escherichia coli over-expressing eut proteins indicates that CD1918 is capable of self-association into arrays, suggesting an organisational role for CD1918 in the formation of this microcompartment. The work presented provides the basis for further study of the architecture and function of the C. difficile eut microcompartment, its role in metabolism and the wider consequences of intestinal colonisation and virulence in this pathogen.
format	article
author	Alison C Pitts Laura R Tuck Alexandra Faulds-Pain Richard J Lewis Jon Marles-Wright
author_facet	Alison C Pitts Laura R Tuck Alexandra Faulds-Pain Richard J Lewis Jon Marles-Wright
author_sort	Alison C Pitts
title	Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.
title_short	Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.
title_full	Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.
title_fullStr	Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.
title_full_unstemmed	Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.
title_sort	structural insight into the clostridium difficile ethanolamine utilisation microcompartment.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/49b1a2d466264d819020a2ff84b62008
work_keys_str_mv	AT alisoncpitts structuralinsightintotheclostridiumdifficileethanolamineutilisationmicrocompartment AT laurartuck structuralinsightintotheclostridiumdifficileethanolamineutilisationmicrocompartment AT alexandrafauldspain structuralinsightintotheclostridiumdifficileethanolamineutilisationmicrocompartment AT richardjlewis structuralinsightintotheclostridiumdifficileethanolamineutilisationmicrocompartment AT jonmarleswright structuralinsightintotheclostridiumdifficileethanolamineutilisationmicrocompartment
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Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.

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