Structural biology study of the ER-associated degradation machinery based on eukaryotic thermophile genomic information

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In this study, we aimed to understand the molecular recognition and operating mechanisms of quality control machineries responsible for the glycoprotein fate determination (folding, transport, and degradation) in the endoplasmic reticulum. Our distinctive approach includes application of the genome information of eukaryotic thermophiles that can grow at high temperature (about 60 degrees Celsius). Using X-ray crystallography, we successfully determined the first crystal structures of protein disulfide isomerase (PDI) catalyzing disulfide bond formation and isomerization, and the catalytic domain of glycoprotein processing enzyme glucosidase II.