Asparagine-linked (N-linked) glycosylation is one of the most common protein modification reactions in eukaryotic cells, occurring upon the majority of proteins that enter the secretory pathway. X-ray crystal structures of the single subunit OSTs from eubacterial and archaebacterial organisms revealed the location of donor and acceptor substrate binding sites and provided the basis for a catalytic mechanism. Cryoelectron microscopy structures of the octameric yeast OST provided substantial insight into the organization and assembly of the multisubunit oligosaccharyltransferases. Furthermore, the cryoelectron microscopy structure of a complex consisting of a mammalian OST complex, the protein translocation channel and a translating ribosome revealed new insight into the mechanism of cotranslational glycosylation.

中文翻译：

---

寡糖基转移酶结构提供了对原核和真核细胞中天冬酰胺连接的糖基化机制的新见解

天冬酰胺连接的（N-连接的）糖基化是真核细胞中最常见的蛋白质修饰反应之一，发生在大多数进入分泌途径的蛋白质上。来自真细菌和古细菌生物的单个亚基OST的X射线晶体结构揭示了供体和受体底物结合位点的位置，并为催化机制提供了基础。八聚体酵母OST的低温电子显微镜结构为多亚基寡糖基转移酶的组织和装配提供了实质性的见识。此外，由哺乳动物OST复合物，蛋白质易位通道和翻译核糖体组成的复合物的低温电子显微镜结构揭示了对共翻译糖基化机制的新见解。