The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbD[alpha] complex

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 (DsbD[alpha]) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction...

Full description

Saved in:
Bibliographic Details
Published in:The EMBO journal 2002-09, Vol.21 (18), p.4774-4784
Main Authors: Haebel, Peter W, Goldstone, David, Katzen, Federico, Beckwith, Jon, Metcalf, Peter
Format: Article
Language:English
Subjects:
E coli
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 (DsbD[alpha]) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbD[alpha] complex. The 2.3 [Angstrom] crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbD[alpha] 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 DsbD[alpha] reveals major conformational changes in a cap structure that regulates the accessibility of the DsbD[alpha] active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
ISSN:0261-4189
1460-2075