Ontology highlight
ABSTRACT:
SUBMITTER: Rozhkova A
PROVIDER: S-EPMC394233 | biostudies-literature | 2004 Apr
REPOSITORIES: biostudies-literature
Rozhkova Anna A Stirnimann Christian U CU Frei Patrick P Grauschopf Ulla U Brunisholz René R Grütter Markus G MG Capitani Guido G Glockshuber Rudi R
The EMBO journal 20040401 8
DsbD from Escherichia coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC. DsbD contains two periplasmically oriented domains at the N- and C-terminus (nDsbD and cDsbD) that are connected by a central transmembrane (TM) domain. Each domain contains a pair of cysteines that are essential for catalysis. Here, we show that Cys109 and Cys461 form a transient interdomain disulfide bond between nDsbD and cDsbD in the reaction cycle of DsbD ...[more]