title: Protein disulfide bond formation in prokaryotes.
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.
authors.affiliation: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. hiroshi_kadokura@hms.harvard.edu
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Kadokura
authors.forename: Federico
authors.initials: F
authors.lastname: Katzen
authors.forename: Jon
authors.initials: J
authors.lastname: Beckwith
mesh_terms: 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
chemical_list: D004220:Disulfides; D008565:Membrane Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; D019704:Protein Disulfide-Isomerases; D003545:Cysteine