1L6P

N-terminal of DsbD (residues 20-144) from E. coli.

Summary for 1L6P

• Entry DOI: 10.2210/pdb1l6p/pdb
• Related: 1JPE
• Descriptor: Thiol:disulfide interchange protein dsbD (2 entities in total)
• Functional Keywords: disulfide bond isomerase protein, immunoglobulin-like fold, electron transport
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P36655
• Total number of polymer chains: 1
• Total formula weight: 14126.69

Authors

Goulding, C.W.,Sawaya, M.R.,Parseghian, A. (deposition date: 2002-03-12, release date: 2002-06-12, Last modification date: 2024-10-30)

Primary citation

Goulding, C.W.,Sawaya, M.R.,Parseghian, A.,Lim, V.,Eisenberg, D.,Missiakas, D.
Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD.
Biochemistry, 41:6920-6927, 2002

PubMed Abstract: Escherichia coli DsbD transports electrons across the plasma membrane, a pathway that leads to the reduction of protein disulfide bonds. Three secreted thioredoxin-like factors, DsbC, DsbE, and DsbG, reduce protein disulfide bonds whereby an active site C-X-X-C motif is oxidized to generate a disulfide bond. DsbD catalyzes the reduction of the disulfide of DsbC, DsbE, and DsbG but not of the thioredoxin-like oxidant DsbA. The reduction of DsbC, DsbE, and DsbG occurs by transport of electrons from cytoplasmic thioredoxin to the C-terminal thioredoxin-like domain of DsbD (DsbD(C)). The N-terminal domain of DsbD, DsbD(N), acts as a versatile adaptor in electron transport and is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD(C). Isolated DsbD(N) is functional in electron transport in vitro. Crystallized DsbD(N) assumes an immunoglobulin-like fold that encompasses two active site cysteines, C103 and C109, forming a disulfide bond between beta-strands. The disulfide of DsbD(N) is shielded from the environment and capped by a phenylalanine (F70). A model is discussed whereby the immunoglobulin fold of DsbD(N) may provide for the discriminating interaction with thioredoxin-like factors, thereby triggering movement of the phenylalanine cap followed by disulfide rearrangement.

PubMed: 12033924
DOI: 10.1021/bi016038l

Experimental method

X-RAY DIFFRACTION (1.65 Å)