Open AccessMutational Alterations of the Key cis Proline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily
Author(s) -
Hiroshi Kadokura,
Lorenzo Nichols,
Jon Beckwith
Publication year - 2005
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.187.4.1519-1522.2005
Subject(s) - dsba , biology , biochemistry , threonine , enzyme , thioredoxin , proline , residue (chemistry) , protein disulfide isomerase , cysteine , serine , amino acid , escherichia coli , gene , periplasmic space
The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins. Conversion of the conserved cis proline 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.