Structural basis of protein disulfide bond generation in the cell

Research output: Contribution to journalReview article

28 Citations (Scopus)

Abstract

The formation of protein disulfide bonds is an oxidative reaction that is crucial for the folding and maturation of many secreted and membrane proteins. Both prokaryotic and eukaryotic cells possess various disulfide oxidoreductases and redox-active cofactors to accelerate this oxidative reaction in a correct manner. Crystal or solution structures have been solved for some of the oxidoreductases in the past 10 years, leading to remarkable progress in the field of thiol-based redox cell biology. Consequently, structural and mechanistic similarities in the disulfide bond formation pathways have been uncovered. This review highlights the molecular basis of the elaborate oxidative systems operating in the Escherichia coli periplasm, the endoplasmic reticulum lumen and the mitochondrial intermembrane space. The accumulated knowledge provides important insights into how protein and redox homeostasis are maintained in the cell.

Original languageEnglish
Pages (from-to)935-943
Number of pages9
JournalGenes to Cells
Volume15
Issue number9
DOIs
Publication statusPublished - 2010 Sep 1
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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