Study on disulfide bond formation protein A in Escherichia coli.
- Author:
Man LUO
1
;
Yi-Xin GUAN
;
Shan-Jing YAO
Author Information
1. Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Disulfides;
chemistry;
metabolism;
Escherichia coli;
enzymology;
genetics;
Escherichia coli Proteins;
chemistry;
classification;
metabolism;
Models, Molecular;
Molecular Sequence Data;
Phylogeny;
Protein Disulfide-Isomerases;
chemistry;
classification;
metabolism;
Protein Folding;
Protein Structure, Tertiary;
Sequence Homology, Amino Acid
- From:
Chinese Journal of Biotechnology
2007;23(1):7-15
- CountryChina
- Language:Chinese
-
Abstract:
Disulfide bond formation protein A, DsbA, is one of the important proteins located in E. coli periplasm, which is a foldase facilitating the folding of nascent secreted proteins, especially for those with many pairs of disulfide bonds. The crystal structure and phylogenetic analysis of DsbA and DsbA-mediated protein folding, alternatively in vivo and in vitro, are summarized. Both the extremely low pKa of Cys30 , about 3.5, and the destabilizing effect of the active site disulfide contribute to its strong oxidizing power. The Cys30 is also considered as the most important residue closely related to its activity using site-directed mutagenesis methodology. DsbA could effectively assist proteins folding, both in vivo coexpressed with the target protein, and in vitro replenished as foldases. Moreover, DsbA also has the chaperone-like activity in the assistant refolding of genetically engineered inclusion bodies.
