1JPE

Crystal structure of DsbD-alpha; the N-terminal domain of DsbD

Summary for 1JPE

• Entry DOI: 10.2210/pdb1jpe/pdb
• Descriptor: DsbD-alpha (2 entities in total)
• Functional Keywords: redox-active center, electron transport, inner membrane, disulfide bond formation
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P36655
• Total number of polymer chains: 1
• Total formula weight: 17091.91

Authors

Haebel, P.W.,Goldstone, D.,Metcalf, P. (deposition date: 2001-08-02, release date: 2002-09-25, Last modification date: 2024-10-30)

Primary citation

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P.
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbD alpha complex.
Embo J., 21:4774-4784, 2002

PubMed Abstract: The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.

PubMed: 12234918
DOI: 10.1093/emboj/cdf489

Experimental method

X-RAY DIFFRACTION (1.9 Å)