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Journal of Biochemistry Advance Access published online on June 29, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp102
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

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Disulfide bond formation system in Eschericia coli

Kenji Inaba*

Division of Protein Chemistry, Post-Genome Science Center, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan

*To whom correspondence should be addressed: Dr. Kenji Inaba, e-mail: inaba-k{at}bioreg.kyushu-u.ac.jp, Tel/Fax: +81-92-642-6433

Received May 9, 2009; Accepted May 14, 2009


  Abstract

The biological kingdoms have evolved elaborate systems that ensure the catalysis of protein disulfide bond formation in the cell. Coexisting in the periplasm of E. coli are the DsbA-DsbB disulfide-introducing and DsbC-DsbD disulfide-isomerizing pathways, which promote the oxidative folding of secreted proteins. Recent structural studies of DsbB have illuminated conformational dynamics involved in the effective oxidation of the extremely reduction-prone oxidase, DsbA, as well as the structure of the reaction center involved in protein disulfide bond formation de novo in conjunction with ubiquinone. Extensive genetic and biochemical analysis has recently provided insight into how DsbD transports electrons from cytosolic thioredoxin to periplasmic DsbC. To a great extent, the molecular mechanisms of the Dsb enzyme system in E. coli have been elucidated, and are applicable to the study of protein disulfide formation systems in other organisms.


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