Protein Family Models

Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. (from Pfam)

Date:

2024-08-14

This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter [1-3]. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD [1-3]. [1]. 12033924. Thiol-disulfide exchange in an immunoglobulin-like fold:. structure of the N-terminal domain of DsbD.. Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D,. Missiakas D;. Biochemistry. 2002;41:6920-6927.. [2]. 29372905. Production, biophysical characterization and initial. crystallization studies of the N- and C-terminal domains of. DsbD, an essential enzyme in Neisseria meningitidis.. Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B;. Acta Crystallogr F Struct Biol Commun. 2018;74:31-38.. [3]. 32305461. Protein Disulfide Exchange by the Intramembrane Enzymes DsbB,. DsbD, and CcdA.. Bushweller JH;. J Mol Biol. 2020;432:5091-5103. (from Pfam)

Date:

2024-08-14

protein-disulfide reductase DsbD family protein, similar to DsbD that facilitates the formation of correct disulfide bonds in some periplasmic proteins and is required for the assembly of the periplasmic c-type cytochromes

Date:

2024-05-08