Protein disulfide bond formation in prokaryotes
Hiroshi Kadokura1, Federico Katzen, Jon Beckwith
1Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. hiroshi_kadokura@hms.harvard.edu
Abstract:
Disulfide bonds formed between pairs of cysteines are important features of the structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia coli to promote the formation of these covalent bonds and to ensure that the correct pairs of cysteines are joined in the final folded protein. These transfers of electrons consist, in the main, of cascades of disulfide bond formation or reduction steps between a series of proteins (DsbA, DsbB, DsbC, and DsbD). A surprising variety of mechanisms and protein structures are involved in carrying out these steps.
Related Concept Videos
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Sulfur Assimilation
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Preparation and Reactions of Thiols
Preparation and Reactions of Sulfides


