Ontology highlight
ABSTRACT:
SUBMITTER: Cho SH
PROVIDER: S-EPMC1948999 | biostudies-literature | 2007 Aug
REPOSITORIES: biostudies-literature
Cho Seung-Hyun SH Porat Amir A Ye Jiqing J Beckwith Jon J
The EMBO journal 20070719 15
The membrane-embedded domain of the unusual electron transporter DsbD (DsbDbeta) uses two redox-active cysteines to catalyze electron transfer between thioredoxin-fold polypeptides on opposite sides of the bacterial cytoplasmic membrane. How the electrons are transferred across the membrane is unknown. Here, we show that DsbDbeta displays an inherent functional and structural symmetry: first, the two cysteines of DsbDbeta can be alkylated from both the cytoplasm and the periplasm. Second, when t ...[more]