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Structural Basis of Disulfide Bond Formation in the Bacterial Periplasm and Mammalian ER

  1. Rieko Kojima,
  2. Masaki Okumura,
  3. Kenji Inaba

Published Online: 19 SEP 2013

DOI: 10.1002/9780470015902.a0024169



How to Cite

Kojima, R., Okumura, M. and Inaba, K. 2013. Structural Basis of Disulfide Bond Formation in the Bacterial Periplasm and Mammalian ER . eLS. .

Author Information

  1. Kyushu University, Division of Protein Chemistry, Medical Institute of Bioregulation, Fukuoka, Japan

  1. Rieko Kojima and Masaki Okumura contributed equally to this review article.

Publication History

  1. Published Online: 19 SEP 2013



Cellular quality control systems rely on the maintenance of protein and redox homoeostasis, in which the formation, reduction and isomerisation of protein disulfide bonds play important roles. The biological kingdoms have evolved catalytic systems that greatly promote oxidative protein folding. Remarkable progress in structural biology in this field has provided molecular views on how protein disulfide bonds are generated de novo and transferred to downstream folding substrates. Very recently, a novel concept has emerged, proposing that multiple oxidative pathways work redundantly, distinctly and in a complementary manner in the endoplasmic reticulum of mammalian cells to efficiently produce large quantities, and a wide variety, of secretory proteins. Thus, the oxidative protein folding network is even more complicated in higher eukaryotes than previously thought.

Key Concepts:

  • Almost all organisms, from bacteria to humans, possess catalytic systems that promote protein-disulfide bond formation.

  • Disulfide bond formation networks have diversified dramatically, as evidenced by the appearance of a large number of disulfide oxidoreductases in higher eukaryotes.

  • High-resolution structures have been solved for an increasing number of disulfide oxidoreductases, thereby revealing the structural and mechanistic basis of cellular disulfide bond formation systems.

  • Disulfide bonds play an important role in folding, assembly and stabilisation of various proteins.

  • Disulfide bond formation networks are closely related to the protein and redox homeostasis in the cell.


  • disulfide bond;
  • crystal structure;
  • DsbA ;
  • DsbB ;
  • PDI ;
  • Ero1;
  • Prx4;
  • GPx;
  • VKOR ;
  • QSOX