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dc.contributor.authorJohnson, Kennetheng
dc.contributor.authorVe, Thomaseng
dc.contributor.authorLarsen, Øivindeng
dc.contributor.authorPedersen, Rolf B.eng
dc.contributor.authorLillehaug, Johan R.eng
dc.contributor.authorJensen, Harald B.eng
dc.contributor.authorHelland, Ronnyeng
dc.contributor.authorKarlsen, Odd Andréeng
dc.description.abstractCorA 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.en_US
dc.rightsAttribution CC BYeng
dc.titleCorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8en_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2014 Johnson et al.en_US
dc.source.journalPLoS ONE

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