The CydDC complex of Escherichia coli is a heterodimeric ATP-binding cassette (ABC) transporter that exports cysteine and glutathione to the periplasm. These reductants are thought to modulate periplasmic redox poise, impacting upon the disulfide folding of periplasmic and secreted proteins involved in bacterial virulence. Diminished CydDC activity abolishes the assembly of functional bd-type respiratory oxidases and perturbs haem ligation during the assembly of c-type cytochromes. The focus herein is upon a newly-discovered interaction of the CydDC complex with a haem cofactor; haem has recently been shown to modulate CydDC activity and structural modelling reveals a potential haem-binding site on the periplasmic surface of the complex. These findings have important implications for future investigations into the potential roles for the CydDC-bound haem in redox sensing and tolerance to nitric oxide (NO).
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October 2015
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Review Article|
October 09 2015
The CydDC ABC transporter of Escherichia coli: new roles for a reductant efflux pump
Mark Shepherd
Mark Shepherd
1
*School of Biosciences, University of Kent, Canterbury, CT2 7NJ, U.K.
1emailM.Shepherd@kent.ac.uk
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Publisher: Portland Press Ltd
Received:
May 01 2015
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2015 Authors; published by Portland Press Limited
2015
Biochem Soc Trans (2015) 43 (5): 908–912.
Article history
Received:
May 01 2015
Citation
Mark Shepherd; The CydDC ABC transporter of Escherichia coli: new roles for a reductant efflux pump. Biochem Soc Trans 1 October 2015; 43 (5): 908–912. doi: https://doi.org/10.1042/BST20150098
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