Protein Disulfide Bond Formation in Prokaryotes
Top Cited Papers
- 1 June 2003
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biochemistry
- Vol. 72 (1) , 111-135
- https://doi.org/10.1146/annurev.biochem.72.121801.161459
Abstract
▪ 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.Keywords
This publication has 108 references indexed in Scilit:
- Randomization of the Entire Active-site Helix α1 of the Thiol-disulfide Oxidoreductase DsbA from Escherichia coliPublished by Elsevier ,2002
- Electron Transfer and Binding of the c-Type Cytochrome TorC to the Trimethylamine N-Oxide Reductase in Escherichia coliJournal of Biological Chemistry, 2001
- Importance of Redox Potential for the in Vivo Function of the Cytoplasmic Disulfide Reductant Thioredoxin from Escherichia coliPublished by Elsevier ,1999
- Characterization of Escherichia coli thioredoxin variants mimicking the active‐sites of other thiol/disulfide oxidoreductasesProtein Science, 1998
- The uncharged surface features surrounding the active site ofEscherichia coliDsbA are conserved and are implicated in peptide bindingProtein Science, 1997
- Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coliGenes to Cells, 1996
- Redox states of DsbA in the periplasm of Escherichia coliFEBS Letters, 1995
- Catalytic Mechanism of DsbA and Its Comparison with That of Protein Disulfide IsomeraseBiochemistry, 1995
- Reactivity and Ionization of the Active Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in vivoBiochemistry, 1994
- The Redox Properties of Protein Disulfide Isomerase (DsbA) of Escherichia coli Result from a Tense Conformation of its Oxidized FormJournal of Molecular Biology, 1993