%0 Journal Article
%T Study on Disulfide Bond Formation Protein A in Escherichia coli
大肠杆菌二硫键形成蛋白A(DsbA)研究进展
%A LUO Man
%A GUAN Yi-Xin
%A YAO Shan-Jing
%A
罗曼
%A 关怡新
%A 姚善泾
%J 生物工程学报
%D 2007
%I
%X 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 pK_a of Cys~ 30 , about 3.5, and the destabilizing effect of the active site disulfide contribute to its strong oxidizing power. The Cys~ 30 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.
%K DsbA
Dsb家族
%K 折叠酶
%K 蛋白质折叠
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=9B52792BD9D7C3A7&yid=A732AF04DDA03BB3&vid=EA389574707BDED3&iid=CA4FD0336C81A37A&sid=DF92D298D3FF1E6E&eid=23CCDDCD68FFCC2F&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=34