Protein Family Models

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:

2024-10-16

This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family. [1]. 7623667. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Crooke H, Cole J;. Mol Microbiol 1995;15:1139-1150. [2]. 7628442. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. Missiakas D, Schwager F, Raina S;. EMBO J 1995;14:3415-3424. (from Pfam)

Date:

2024-10-16

Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise. (from Pfam)

Date:

2024-08-14

Gene:

dsbD

Date:

2021-08-05