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The CydDC ABC transporter of Escherichia coli: new roles for a reductant efflux pump

Shepherd, M. (2015) The CydDC ABC transporter of Escherichia coli: new roles for a reductant efflux pump. Biochemical Society Transactions, 43 (5). pp. 908-912. ISSN 0300-5127. (doi:10.1042/BST20150098) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:51037)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1042/BST20150098

Abstract

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).

Item Type: Article
DOI/Identification number: 10.1042/BST20150098
Subjects: Q Science > QR Microbiology
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Mark Shepherd
Date Deposited: 15 Oct 2015 13:09 UTC
Last Modified: 23 Jan 2020 04:10 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/51037 (The current URI for this page, for reference purposes)
Shepherd, M.: https://orcid.org/0000-0002-7472-2300
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