| Budget Amount *help |
¥18,070,000 (Direct Cost: ¥13,900,000、Indirect Cost: ¥4,170,000)
Fiscal Year 2014: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2013: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2012: ¥6,500,000 (Direct Cost: ¥5,000,000、Indirect Cost: ¥1,500,000)
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| Outline of Final Research Achievements |
The addition of oligosaccharide chains on the asparagine residues in proteins is catalyzed by the membrane enzyme, oligosaccharyltransferase (OST). We determined the crystal structures of the C-terminal globular domains and the full-length OST protein from hyperthermophilic archaea. We also showed that the dynamic feature of the C-terminal globular domains was essential for the oligosaccharyl transfer activity. The crystal structure in the complex with the oligosaccharide acceptor substrate was determined using the tethering of a peptide containing the Asn-Val-Thr sequon to the protein through a disulfide bond. Toward the determination of the complex structure with the oligosaccharide donor substrate, we analyzed the chemical structures of archaeal lipid-linked oligosaccharides to synthesize the water-soluble analogues.
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