ArticleThe Journal of biological chemistry2014
Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Heme utilization by the enterococci.FEMS microbes · 2024Review
- Cryo-EM structures of a prokaryotic heme transporter CydDC.Protein & cell · 2023Article
- Dissecting the conformational complexity and mechanism of a bacterial heme transporter.Nature chemical biology · 2023Article
- Heme cross-feeding can augment Staphylococcus aureus and Enterococcus faecalis dual species biofilms.The ISME journal · 2022Article
- A DasA family sugar binding protein Ste2 links nutrient and oxidative stress to exopolysaccharides production in Streptomyces sp. 139.BMC microbiology · 2022Article
- Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021Review
- CydDC functions as a cytoplasmic cystine reductase to sensitizeProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Restoration of biofuel production levels and increased tolerance under ionic liquid stress is enabled by a mutation in the essential Escherichia coli gene cydC.Microbial cell factories · 2018Article
- A heme-binding domain controls regulation of ATP-dependent potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- CydDC-mediated reductant export in Escherichia coli controls the transcriptional wiring of energy metabolism and combats nitrosative stress.The Biochemical journal · 2016Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ATP-binding cassette-type cysteine/GSH transporter, CydDC. Recombinant CydDC was purified as a heterodimer and found to be an active ATPase both in soluble form with detergent and when reconstituted into a lipid environment. Two-dimensional crystals of CydDC were analyzed by electron cryomicroscopy, and the protein was shown to be made up of two non-identical domains corresponding to the putative CydD and CydC subunits, with dimensions characteristic of other ATP-binding cassette transporters. CydDC binds heme b. Detergent-solubilized CydDC appears to adopt at least two structural states, each associated with a characteristic level of bound heme. The purified protein in detergent showed a weak basal ATPase activity (approximately 100 nmol Pi/min/mg) that was stimulated ∼3-fold by various thiol compounds, suggesting that CydDC could act as a thiol transporter. The presence of heme (either intrinsic or added in the form of hemin) led to a further enhancement of thiol-stimulated ATPase activity, although a large excess of heme inhibited activity. Similar responses of the ATPase activity were observed with CydDC reconstituted into E. coli lipids. These results suggest that heme may have a regulatory role in CydDC-mediated transmembrane thiol transport.
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