Functional differences between human and yeast protein disulfide isomerase family proteins

2004 ◽  
Vol 320 (2) ◽  
pp. 359-365 ◽  
Author(s):  
Taiji Kimura ◽  
Yasuhiro Hosoda ◽  
Yukiko Kitamura ◽  
Hideshi Nakamura ◽  
Tomohisa Horibe ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Yeast Protein ◽  
Disulfide Isomerase ◽  
Functional Differences ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

scholarly journals Structure-Function Analysis of the Endoplasmic Reticulum Oxidoreductase TMX3 Reveals Interdomain Stabilization of the N-terminal Redox-active Domain

2007 ◽  
Vol 282 (46) ◽  
pp. 33859-33867 ◽  
Author(s):  
Johannes Haugstetter ◽  
Michael Andreas Maurer ◽  
Thomas Blicher ◽  
Martin Pagac ◽  
Gerhard Wider ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Function Analysis ◽  
Transmembrane Protein ◽  
Reduced Form ◽  
Disulfide Isomerase ◽  
Binding Domains ◽  
Redox Active ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

Disulfide bond formation in the endoplasmic reticulum is catalyzed by enzymes of the protein disulfide-isomerase family that harbor one or more thioredoxin-like domains. We recently discovered the transmembrane protein TMX3, a thiol-disulfide oxidoreductase of the protein disulfide-isomerase family. Here, we show that the endoplasmic reticulum-luminal region of TMX3 contains three thioredoxin-like domains, an N-terminal redox-active domain (named a) followed by two enzymatically inactive domains (b and b′). Using the recombinantly expressed TMX3 domain constructs a, ab, and abb′, we compared structural stability and enzymatic properties. By structural and biophysical methods, we demonstrate that the reduced a domain has features typical of a globular folded domain that is, however, greatly destabilized upon oxidization. Importantly, interdomain stabilization by the b domain renders the a domain more resistant toward chemical denaturation and proteolysis in both the oxidized and reduced form. In combination with molecular modeling studies of TMX3 abb′, the experimental results provide a new understanding of the relationship between the multidomain structure of TMX3 and its function as a redox enzyme. Overall, the data indicate that in addition to their role as substrate and co-factor binding domains, redox-inactive thioredoxin-like domains also function in stabilizing neighboring redox-active domains.

scholarly journals Inhibitors of the protein disulfide isomerase family for the treatment of multiple myeloma

Leukemia ◽  
2018 ◽  
Vol 33 (4) ◽  
pp. 1011-1022 ◽  
Author(s):  
Reeder M. Robinson ◽  
Leticia Reyes ◽  
Ravyn M. Duncan ◽  
Haiyan Bian ◽  
Allen B. Reitz ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

scholarly journals The Crystal Structure of the Protein-Disulfide Isomerase Family Member ERp27 Provides Insights into Its Substrate Binding Capabilities

2012 ◽  
Vol 288 (3) ◽  
pp. 2029-2039 ◽  
Author(s):  
Franz-Xaver Kober ◽  
Wolfgang Koelmel ◽  
Jochen Kuper ◽  
Johannes Drechsler ◽  
Christine Mais ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Family Member ◽  
Protein Disulfide Isomerase ◽  
Substrate Binding ◽  
Disulfide Isomerase ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

Yeast Mpd1p Reveals the Structural Diversity of the Protein Disulfide Isomerase Family

2008 ◽  
Vol 384 (3) ◽  
pp. 631-640 ◽  
Author(s):  
Elvira Vitu ◽  
Einav Gross ◽  
Harry M. Greenblatt ◽  
Carolyn S. Sevier ◽  
Chris A. Kaiser ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Structural Diversity ◽  
Disulfide Isomerase ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family
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