User:Nhi Pham/Sandbox 1
From Proteopedia
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== Introduction == | == Introduction == | ||
| - | N-linked glycosylation is an essential process in protein modification. This form of glycosylation is important in the folding and sorting of proteins in the endoplasmic reticulum (ER) and the interaction between proteins and cells. <ref>DOI 10.1038/nature25755</ref> In humans, N-linked glycosylation is catalyzed co-translationally by an enzyme complex called oligosaccharyltransferase complex A (OST-A) in the rough ER. This means that the peptide chain is glycosylated by this complex as it is synthesized by the ribosome and enters the ER lumen through translocon protein Sec61.<ref name=" | + | N-linked glycosylation is an essential process in protein modification. This form of glycosylation is important in the folding and sorting of proteins in the endoplasmic reticulum (ER) and the interaction between proteins and cells. <ref name="Bai2018">DOI 10.1038/nature25755</ref> In humans, N-linked glycosylation is catalyzed co-translationally by an enzyme complex called oligosaccharyltransferase complex A (OST-A) in the rough ER. This means that the peptide chain is glycosylated by this complex as it is synthesized by the ribosome and enters the ER lumen through translocon protein Sec61.<ref name="Lu">DOI 10.1073/pnas.1806034115</ref> As suggested by the name, this enzyme complex transfers the high mannose fourteen-sugar chain from a lipid-linked oligosaccharide donor containing dolichol pyrophosphate to the peptide chain containing the Asn-X-Thr (N-X-T) sequence, where X is any amino acid but not Proline.<ref name="Bai2018"/> In addition, this enzyme complex is also part of the glycosyltransferase-C (GT-C) fold, which is a protein that has a transmembrane helical domain and a mix of α/β soluble domains (Bai and Li 2019).<ref name="Bai2019">DOI 10.1111/febs.14705</ref> On this page, the structure of the OST-A and its components; its mechanism, and diseases associated with this complex are discussed. |
== Structure == | == Structure == | ||
Revision as of 17:57, 21 April 2022
Human Oligosaccharyltransferase complex A (OST-A)
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ 3.0 3.1 Bai L, Wang T, Zhao G, Kovach A, Li H. The atomic structure of a eukaryotic oligosaccharyltransferase complex. Nature. 2018 Jan 22. pii: nature25755. doi: 10.1038/nature25755. PMID:29466327 doi:http://dx.doi.org/10.1038/nature25755
- ↑ Lu H, Fermaintt CS, Cherepanova NA, Gilmore R, Yan N, Lehrman MA. Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis. Proc Natl Acad Sci U S A. 2018 Sep 18;115(38):9557-9562. doi:, 10.1073/pnas.1806034115. Epub 2018 Sep 4. PMID:30181269 doi:http://dx.doi.org/10.1073/pnas.1806034115
- ↑ Bai L, Li H. Cryo-EM is uncovering the mechanism of eukaryotic protein N-glycosylation. FEBS J. 2019 May;286(9):1638-1644. doi: 10.1111/febs.14705. Epub 2018 Dec 3. PMID:30450807 doi:http://dx.doi.org/10.1111/febs.14705
