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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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2021-11-01
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| Series: | PLoS Biology |
| Online Access: | https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.3001446&type=printable |
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| 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 |
| collection | DOAJ |
| 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 |
| id | doaj-art-af8157dec86e4154a2b6cbf9055eb196 |
| institution | Kabale University |
| issn | 1544-9173 1545-7885 |
| language | English |
| publishDate | 2021-11-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj-art-af8157dec86e4154a2b6cbf9055eb1962025-08-20T03:25:34ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852021-11-011911e300144610.1371/journal.pbio.3001446Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.Satya Prathyusha BhamidimarriTessa R YoungMuralidharan ShanmugamSandra SoderholmArnaud BasléDirk BumannBert van den BergCopper, 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.https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.3001446&type=printable |
| spellingShingle | 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. PLoS Biology |
| title | 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_short | 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 |
| url | https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.3001446&type=printable |
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