CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.

CorA is a copper repressible protein previously identified in the methanotrophic bacterium Methylomicrobium album BG8. In this work, we demonstrate that CorA is located on the cell surface and binds one copper ion per protein molecule, which, based on X-ray Absorption Near Edge Structure analysis, i...

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Autores principales:	Kenneth A Johnson, Thomas Ve, Oivind Larsen, Rolf B Pedersen, Johan R Lillehaug, Harald B Jensen, Ronny Helland, Odd A Karlsen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6f852697dc74462c812ad7964fb6f004
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spelling	oai:doaj.org-article:6f852697dc74462c812ad7964fb6f0042021-11-18T08:34:11ZCorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.1932-620310.1371/journal.pone.0087750https://doaj.org/article/6f852697dc74462c812ad7964fb6f0042014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24498370/?tool=EBIhttps://doaj.org/toc/1932-6203CorA is a copper repressible protein previously identified in the methanotrophic bacterium Methylomicrobium album BG8. In this work, we demonstrate that CorA is located on the cell surface and binds one copper ion per protein molecule, which, based on X-ray Absorption Near Edge Structure analysis, is in the reduced state (Cu(I)). The structure of endogenously expressed CorA was solved using X-ray crystallography. The 1.6 Å three-dimensional structure confirmed the binding of copper and revealed that the copper atom was coordinated in a mononuclear binding site defined by two histidines, one water molecule, and the tryptophan metabolite, kynurenine. This arrangement of the copper-binding site is similar to that of its homologous protein MopE* from Metylococcus capsulatus Bath, confirming the importance of kynurenine for copper binding in these proteins. Our findings show that CorA has an overall fold similar to MopE, including the unique copper(I)-binding site and most of the secondary structure elements. We suggest that CorA plays a role in the M. album BG8 copper acquisition.Kenneth A JohnsonThomas VeOivind LarsenRolf B PedersenJohan R LillehaugHarald B JensenRonny HellandOdd A KarlsenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 2, p e87750 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kenneth A Johnson Thomas Ve Oivind Larsen Rolf B Pedersen Johan R Lillehaug Harald B Jensen Ronny Helland Odd A Karlsen CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
description	CorA is a copper repressible protein previously identified in the methanotrophic bacterium Methylomicrobium album BG8. In this work, we demonstrate that CorA is located on the cell surface and binds one copper ion per protein molecule, which, based on X-ray Absorption Near Edge Structure analysis, is in the reduced state (Cu(I)). The structure of endogenously expressed CorA was solved using X-ray crystallography. The 1.6 Å three-dimensional structure confirmed the binding of copper and revealed that the copper atom was coordinated in a mononuclear binding site defined by two histidines, one water molecule, and the tryptophan metabolite, kynurenine. This arrangement of the copper-binding site is similar to that of its homologous protein MopE* from Metylococcus capsulatus Bath, confirming the importance of kynurenine for copper binding in these proteins. Our findings show that CorA has an overall fold similar to MopE, including the unique copper(I)-binding site and most of the secondary structure elements. We suggest that CorA plays a role in the M. album BG8 copper acquisition.
format	article
author	Kenneth A Johnson Thomas Ve Oivind Larsen Rolf B Pedersen Johan R Lillehaug Harald B Jensen Ronny Helland Odd A Karlsen
author_facet	Kenneth A Johnson Thomas Ve Oivind Larsen Rolf B Pedersen Johan R Lillehaug Harald B Jensen Ronny Helland Odd A Karlsen
author_sort	Kenneth A Johnson
title	CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
title_short	CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
title_full	CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
title_fullStr	CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
title_full_unstemmed	CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
title_sort	cora is a copper repressible surface-associated copper(i)-binding protein produced in methylomicrobium album bg8.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/6f852697dc74462c812ad7964fb6f004
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CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.

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