Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.

Copper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it...

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Autores principales:	Satya Prathyusha Bhamidimarri, Tessa R Young, Muralidharan Shanmugam, Sandra Soderholm, Arnaud Baslé, Dirk Bumann, Bert van den Berg
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/af8157dec86e4154a2b6cbf9055eb196
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spelling	oai:doaj.org-article:af8157dec86e4154a2b6cbf9055eb1962021-12-02T19:54:43ZAcquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.1544-91731545-788510.1371/journal.pbio.3001446https://doaj.org/article/af8157dec86e4154a2b6cbf9055eb1962021-11-01T00:00:00Zhttps://doi.org/10.1371/journal.pbio.3001446https://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Copper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it is still unclear whether and how gram-negative bacteria acquire ionic copper. Here, we show that Pseudomonas aeruginosa OprC is an outer membrane, TonB-dependent transporter that is conserved in many Proteobacteria and which mediates acquisition of both reduced and oxidised ionic copper via an unprecedented CxxxM-HxM metal binding site. Crystal structures of wild-type and mutant OprC variants with silver and copper suggest that acquisition of Cu(I) occurs via a surface-exposed "methionine track" leading towards the principal metal binding site. Together with whole-cell copper quantitation and quantitative proteomics in a murine lung infection model, our data identify OprC as an abundant component of bacterial copper biology that may enable copper acquisition under a wide range of conditions.Satya Prathyusha BhamidimarriTessa R YoungMuralidharan ShanmugamSandra SoderholmArnaud BasléDirk BumannBert van den BergPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 19, Iss 11, p e3001446 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Satya Prathyusha Bhamidimarri Tessa R Young Muralidharan Shanmugam Sandra Soderholm Arnaud Baslé Dirk Bumann Bert van den Berg Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
description	Copper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it is still unclear whether and how gram-negative bacteria acquire ionic copper. Here, we show that Pseudomonas aeruginosa OprC is an outer membrane, TonB-dependent transporter that is conserved in many Proteobacteria and which mediates acquisition of both reduced and oxidised ionic copper via an unprecedented CxxxM-HxM metal binding site. Crystal structures of wild-type and mutant OprC variants with silver and copper suggest that acquisition of Cu(I) occurs via a surface-exposed "methionine track" leading towards the principal metal binding site. Together with whole-cell copper quantitation and quantitative proteomics in a murine lung infection model, our data identify OprC as an abundant component of bacterial copper biology that may enable copper acquisition under a wide range of conditions.
format	article
author	Satya Prathyusha Bhamidimarri Tessa R Young Muralidharan Shanmugam Sandra Soderholm Arnaud Baslé Dirk Bumann Bert van den Berg
author_facet	Satya Prathyusha Bhamidimarri Tessa R Young Muralidharan Shanmugam Sandra Soderholm Arnaud Baslé Dirk Bumann Bert van den Berg
author_sort	Satya Prathyusha Bhamidimarri
title	Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
title_short	Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
title_full	Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
title_fullStr	Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
title_full_unstemmed	Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
title_sort	acquisition of ionic copper by the bacterial outer membrane protein oprc through a novel binding site.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/af8157dec86e4154a2b6cbf9055eb196
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Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.

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