CorA Is a Copper Repressible Surface-Associated Copper(I)-Binding Protein Produced in Methylomicrobium album BG8

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Author(s)
Johnson, Kenneth A
Ve, Thomas
Larsen, Oivind
Pedersen, Rolf B
Lillehaug, Johan R
Jensen, Harald B
Helland, Ronny
Karlsen, Odd A
Griffith University Author(s)
Year published
2014
Metadata
Show full item recordAbstract
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 proteinmolecule, 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 A°
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 ...
View more >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 proteinmolecule, 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 A° 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.
View less >
View more >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 proteinmolecule, 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 A° 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.
View less >
Journal Title
PLoS One
Volume
9
Issue
2
Copyright Statement
© 2014 Johnson et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits
unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Subject
Biochemistry and Cell Biology not elsewhere classified