Protein disulfide bond formation in prokaryotes.
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.
Kadokura
Hiroshi
H
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. hiroshi_kadokura@hms.harvard.edu
Katzen
Federico
F
Beckwith
Jon
J
D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism*; D004579:Electron Transport; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010088:Oxidoreductases / Q000378:metabolism; D019897:Periplasm / Q000378:metabolism; D011387:Prokaryotic Cells / Q000201:enzymology / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D013879:Thioredoxins / Q000737:chemistry / Q000378:metabolism
D004220:Disulfides; D008565:Membrane Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; D019704:Protein Disulfide-Isomerases; D003545:Cysteine