![]() In the lower scheme, the sampling of an open conformation by nDsbD allows formation of the complex without steric clashes. In the upper scheme, a steric clash upon binding induces cap loop opening. ( D) The central panels illustrate two possible mechanisms mediating cap loop opening in the formation of the nDsbD-cDsbD complex. ( C) Schematic representation of the thiol-disulfide exchange reaction (bimolecular nucleophilic substitution) between cDsbD and nDsbD. Oxidized DsbC, CcmG and DsbG subsequently accept electrons from nDsbD red. Trx red reduces the disulfide bond in tmDsbD ox, tmDsbD red then reduces cDsbD ox, and cDsbD red subsequently reduces nDsbD ox. Two electrons and two H + are transferred in each step. ![]() ( B) Electron transfer reactions involving DsbD are shown. nDsbD and cDsbD are shown in cyan and grey, respectively. cDsbD, DsbC, CcmG and DsbG have a thioredoxin fold (circle), typical of thiol-disulfide oxidoreductases, while nDsbD adopts an immunoglobulin fold (square). ( A) DsbD comprises a central domain with eight transmembrane helices (tmDsbD) and two periplasmic globular domains (nDsbD and cDsbD). The electron transfer pathway from thioredoxin (Trx) to periplasmic partner proteins is shown.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |