Mutational Alterations of the KeycisProline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily
Open Access
- 15 February 2005
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 187 (4) , 1519-1522
Abstract
The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins. Conversion of the conservedcisproline 151 of DsbA to several hydrophilic residues results in accumulation of mixed disulfides between DsbA and its dedicated oxidant, DsbB. However, only a proline-to-threonine change causes accumulation of mixed disulfides of DsbA with its substrates.Keywords
This publication has 33 references indexed in Scilit:
- DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA OxidationJournal of Biological Chemistry, 2004
- The Influence of His94 and Pro149 in Modulating the Activity of V. cholerae DsbAAntioxidants & Redox Signaling, 2003
- Protein Disulfide Bond Formation in ProkaryotesAnnual Review of Biochemistry, 2003
- On the role of the cis‐proline residue in the active site of DsbAProtein Science, 1999
- The uncharged surface features surrounding the active site ofEscherichia coliDsbA are conserved and are implicated in peptide bindingProtein Science, 1997
- The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversalStructure, 1996
- DsbA-DsbB Interaction through Their Active Site CysteinesJournal of Biological Chemistry, 1995
- 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
- Identification of a protein required for disulfide bond formation in vivoCell, 1991