This entry consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity [2]. In eukaryotes, OTase transfers a l ...
This entry consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity [2]. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER [2]. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines [3-4]. This entry represents the N-terminal domain, consisting of transmembrane helices.
This entry represents the C-terminal core domain found in the oligosaccharyl transferase STT3 subunit and related proteins, such as bacterial PglB and archaeal AlgB. STT3 is part of the oligosccharyl transferase (OTase) complex and required for its a ...
This entry represents the C-terminal core domain found in the oligosaccharyl transferase STT3 subunit and related proteins, such as bacterial PglB and archaeal AlgB. STT3 is part of the oligosccharyl transferase (OTase) complex and required for its activity, which transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines [1-5]. This is a globular domain which adopts a mixed alpha/beta fold and contains the highly conserved WWDYG motif, in which the aspartate residue is thought to function as a catalytic residue [1-5].
Members of this entry are involved in asparagine-linked protein glycosylation. In particular, dolichyl-diphosphooligosaccharide-protein glycosyltransferase (DDOST), also known as oligosaccharyltransferase, transfers the high-mannose sugar GlcNAc(2)-M ...
Members of this entry are involved in asparagine-linked protein glycosylation. In particular, dolichyl-diphosphooligosaccharide-protein glycosyltransferase (DDOST), also known as oligosaccharyltransferase, transfers the high-mannose sugar GlcNAc(2)-Man(9)-Glc(3) from a dolichol-linked donor to an asparagine acceptor in a consensus Asn-X-Ser/Thr motif. In most eukaryotes, the DDOST complex is composed of three subunits, which in humans are described as a 48kD subunit, ribophorin I, and ribophorin II. However, the yeast DDOST appears to consist of six subunits (alpha, beta, gamma, delta, epsilon, zeta). The yeast beta subunit is a 45kD polypeptide, previously discovered as the Wbp1 protein, with known sequence similarity to the human 48kD subunit and the other orthologues. This is the N-terminal domain of OST48 subunits from animals and plants and the orthologue from yeast Wbp1. This domain is distantly related to the IFT52 N-terminal domain (Pfam:PF23355).