FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W3016692850> ?p ?o ?g. }

• W3016692850 endingPage "624" @default.
• W3016692850 startingPage "624" @default.
• W3016692850 abstract "Asparagine-linked glycosylation, also known as N-linked glycosylation is an essential and highly conserved post-translational protein modification that occurs in all three domains of life. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell–cell communication, and stability. Defects in N-linked glycosylation results in a class of inherited diseases known as congenital disorders of glycosylation (CDG). N-linked glycosylation occurs in the endoplasmic reticulum (ER) lumen by a membrane associated enzyme complex called the oligosaccharyltransferase (OST). In the central step of this reaction, an oligosaccharide group is transferred from a lipid-linked dolichol pyrophosphate donor to the acceptor substrate, the side chain of a specific asparagine residue of a newly synthesized protein. The prokaryotic OST enzyme consists of a single polypeptide chain, also known as single subunit OST or ssOST. In contrast, the eukaryotic OST is a complex of multiple non-identical subunits. In this review, we will discuss the biochemical and structural characterization of the prokaryotic, yeast, and mammalian OST enzymes. This review explains the most recent high-resolution structures of OST determined thus far and the mechanistic implication of N-linked glycosylation throughout all domains of life. It has been shown that the ssOST enzyme, AglB protein of the archaeon Archaeoglobus fulgidus, and the PglB protein of the bacterium Campylobactor lari are structurally and functionally similar to the catalytic Stt3 subunit of the eukaryotic OST enzyme complex. Yeast OST enzyme complex contains a single Stt3 subunit, whereas the human OST complex is formed with either STT3A or STT3B, two paralogues of Stt3. Both human OST complexes, OST-A (with STT3A) and OST-B (containing STT3B), are involved in the N-linked glycosylation of proteins in the ER. The cryo-EM structures of both human OST-A and OST-B complexes were reported recently. An acceptor peptide and a donor substrate (dolichylphosphate) were observed to be bound to the OST-B complex whereas only dolichylphosphate was bound to the OST-A complex suggesting disparate affinities of two OST complexes for the acceptor substrates. However, we still lack an understanding of the independent role of each eukaryotic OST subunit in N-linked glycosylation or in the stabilization of the enzyme complex. Discerning the role of each subunit through structure and function studies will potentially reveal the mechanistic details of N-linked glycosylation in higher organisms. Thus, getting an insight into the requirement of multiple non-identical subunits in the N-linked glycosylation process in eukaryotes poses an important future goal." @default.
• W3016692850 created "2020-04-24" @default.
• W3016692850 creator A5068534341 @default.
• W3016692850 creator A5079209474 @default.
• W3016692850 creator A5082496642 @default.
• W3016692850 date "2020-04-17" @default.
• W3016692850 modified "2023-10-18" @default.
• W3016692850 title "Structural Insight into the Mechanism of N-Linked Glycosylation by Oligosaccharyltransferase" @default.
• W3016692850 cites W142386558 @default.
• W3016692850 cites W1481014269 @default.
• W3016692850 cites W1525601872 @default.
• W3016692850 cites W1528516857 @default.
• W3016692850 cites W1534242591 @default.
• W3016692850 cites W1588330609 @default.
• W3016692850 cites W1674185300 @default.
• W3016692850 cites W1678965935 @default.
• W3016692850 cites W1947454816 @default.
• W3016692850 cites W1964462261 @default.
• W3016692850 cites W1964973871 @default.
• W3016692850 cites W1973505268 @default.
• W3016692850 cites W1976104570 @default.
• W3016692850 cites W1979260907 @default.
• W3016692850 cites W1982675033 @default.
• W3016692850 cites W1984646810 @default.
• W3016692850 cites W1987804131 @default.
• W3016692850 cites W1990133186 @default.
• W3016692850 cites W1991344063 @default.
• W3016692850 cites W1992749363 @default.
• W3016692850 cites W1994089342 @default.
• W3016692850 cites W1998274788 @default.
• W3016692850 cites W2001929483 @default.
• W3016692850 cites W2006005895 @default.
• W3016692850 cites W2015041810 @default.
• W3016692850 cites W2016501272 @default.
• W3016692850 cites W2019894781 @default.
• W3016692850 cites W2024451651 @default.
• W3016692850 cites W2026013020 @default.
• W3016692850 cites W2026712108 @default.
• W3016692850 cites W2027390719 @default.
• W3016692850 cites W2031894550 @default.
• W3016692850 cites W2032719065 @default.
• W3016692850 cites W2033132059 @default.
• W3016692850 cites W2033319529 @default.
• W3016692850 cites W2034791373 @default.
• W3016692850 cites W2040953890 @default.
• W3016692850 cites W2045897529 @default.
• W3016692850 cites W2046916214 @default.
• W3016692850 cites W2050046181 @default.
• W3016692850 cites W2057487309 @default.
• W3016692850 cites W2059231773 @default.
• W3016692850 cites W2063097466 @default.
• W3016692850 cites W2066825192 @default.
• W3016692850 cites W2066928778 @default.
• W3016692850 cites W2068454258 @default.
• W3016692850 cites W2068663593 @default.
• W3016692850 cites W2070926743 @default.
• W3016692850 cites W2072265501 @default.
• W3016692850 cites W2076117904 @default.
• W3016692850 cites W2077417665 @default.
• W3016692850 cites W2082050815 @default.
• W3016692850 cites W2082693434 @default.
• W3016692850 cites W2085648696 @default.
• W3016692850 cites W2086030298 @default.
• W3016692850 cites W2088221752 @default.
• W3016692850 cites W2101544545 @default.
• W3016692850 cites W2102909508 @default.
• W3016692850 cites W2103137962 @default.
• W3016692850 cites W2106203560 @default.
• W3016692850 cites W2115380390 @default.
• W3016692850 cites W2116520360 @default.
• W3016692850 cites W2123142240 @default.
• W3016692850 cites W2123658589 @default.
• W3016692850 cites W2124106344 @default.
• W3016692850 cites W2127324121 @default.
• W3016692850 cites W2132089800 @default.
• W3016692850 cites W2138081057 @default.
• W3016692850 cites W2145832204 @default.
• W3016692850 cites W2149369491 @default.
• W3016692850 cites W2149846461 @default.
• W3016692850 cites W2150764734 @default.
• W3016692850 cites W2152708819 @default.
• W3016692850 cites W2154369501 @default.
• W3016692850 cites W2154631099 @default.
• W3016692850 cites W2157402334 @default.
• W3016692850 cites W2161171034 @default.
• W3016692850 cites W2167835857 @default.
• W3016692850 cites W2167879508 @default.
• W3016692850 cites W2175847082 @default.
• W3016692850 cites W2309952403 @default.
• W3016692850 cites W2338225276 @default.
• W3016692850 cites W2566131830 @default.
• W3016692850 cites W2615423370 @default.
• W3016692850 cites W2735791150 @default.
• W3016692850 cites W2751799886 @default.
• W3016692850 cites W2765461328 @default.
• W3016692850 cites W2782128418 @default.
• W3016692850 cites W2784678659 @default.
• W3016692850 cites W2792177065 @default.

• next