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Oligosaccharyltransferase or OST (EC 126.96.36.199) is a membrane protein complex that transfers a 14-sugar oligosaccharide from dolichol to nascent protein. It is a type of glycosyltransferase. The sugar Glc3Man9GlcNAc2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) residue in the sequence Asn-X-Ser or Asn-X-Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked glycosylation pathway.
Additional recommended knowledge
OST is a component of the translocon in the endoplasmic reticulum (ER) membrane. The active site of OST is located about 4 nm from the lumenal face of the ER membrane . It usually acts during translation as the nascent protein is entering the ER, but this cotranslational glycosylation is nevertheless called a posttranslational modification. A few examples have been found of OST activity after translation is complete , . Current opinion is that post-translational activity may occur if the protein is poorly folded or folds slowly .
Structure and function
Yeast OST is composed of eight different membrane-spanning proteins in three subcomplexesoligomers, and three of the eight proteins are glycosylated themselves , . OST in mammals is known to have a similar composition ., . These octomers do not form higher order
OST is thought to require many subunits because it must:
Congenital disorders of glycosylation (CDG) types
CDG syndromes are genetic disorders of the glycosylation pathway. They are labelled "Type I" if the defective gene is for an enzyme involved in the assembly or transfer of the Glc3Man9GlcNAc2-dolichol precursor. They are labelled "Type II" if the defective step occurs after the action of OST in the N-linked glyocsylation pathway or involves O-linked glycosylation.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Oligosaccharyltransferase". A list of authors is available in Wikipedia.|