oligosaccharyltransferase forms a binary complex with ribosomes. Reconstitution of a binary complex containing oligosaccharyltransferase and ribosomes and its electron microscopic images. Oligosaccharyltransferase, the Sec61 complex, and ribosomes form a ternary complex in vitro
multiple oligosaccharyl transferase isoforms with different affinities for the translocon and ribosome and with heterogeneous subunit composition might exist in the endoplasmic reticulum membrane, thereby providing a means of regulating protein N-glycosylation
oligosaccharyl transferase has a large domain in the lumenal side of endoplasmic reticulum where the catalysis occurs. The lumenal domain mainly comprises the catalytic Stt3p, the donor substrate-recognizing Wbp1p, and the acceptor substrate-recognizing Ost1p
oligosaccharyl transferase has a large domain in the lumenal side of endoplasmic reticulum where the catalysis occurs. The lumenal domain mainly comprises the catalytic Stt3p, the donor substrate-recognizing Wbp1p, and the acceptor substrate-recognizing Ost1p
OST48, ribophorin I and ribophorin II possess a type I membrane topology with the bulk of their polypeptide chains directed to towards the lumen of the endoplasmic reticulum
membrane protein complex. Ost2p and Stt3p have only their N terminus located in the cytosol. Ost3p and Swp1p have only their C terminus oriented in the cytosol. In the case of Ost5p and Ost6p, both their N and C termini are present in the cytosol
multiple oligosaccharyl transferase isoforms with different affinities for the translocon and ribosome and with heterogeneous subunit composition might exist in the endoplasmic reticulum membrane, thereby providing a means of regulating protein N-glycosylation
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Ost4p is a minimembrane protein
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Ost5p is a membrane protein
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Swp1p probably possesses three transmembrane segments, with its N-terminus in the lumen and C-terminus in the cytosol
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The functional domain of Ost1p is its membrane-anchored lumenal domain
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The Ost2 protein possesses three transmembrane segments, with its N-terminus in the cytosol and C-terminus directed towards the lumen
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The sequence of the lumen-oriented half of the transmembrane domain is important for the function of the Wbp1 protein
OST48, ribophorin I and ribophorin II possess a type I membrane topolyogy with the bulk of their polypeptide chains directed towards the lumen of the endoplasmic reticulum