User:Nhi Pham/Sandbox 1

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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 (Bai et. al., 2018)<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 (Lu et. al., 2018). 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 (Bai et.al., 2019). 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). On this page, the structure of the OST-A and its components; its mechanism, and diseases associated with this complex are discussed.
	== Structure ==		== Structure ==

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Revision as of 17:36, 21 April 2022

Human Oligosaccharyltransferase complex A (OST-A)

spinqualitylabelsall models The structure of the oligosaccharyltransferase complex A (OST-A) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image This is a default text for your page Nhi Pham/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. 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 (Bai et. al., 2018)[3]

References

1. ↑ 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
2. ↑ 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. ↑ doi: https://dx.doi.org/10.1038/nature25755<ref>.Inhumans,N-linkedglycosylationiscatalyzedco-translationallybyanenzymecomplexcalledoligosaccharyltransferasecomplexA(OST-A)intheroughER.ThismeansthatthepeptidechainisglycosylatedbythiscomplexasitissynthesizedbytheribosomeandenterstheERlumenthroughtransloconproteinSec61(Luet.al.,2018).Assuggestedbythename,thisenzymecomplextransfersthehighmannosefourteen-sugarchainfromalipid-linkedoligosaccharidedonorcontainingdolicholpyrophosphatetothepeptidechaincontainingtheAsn-X-Thr(N-X-T)sequence,whereXisanyaminoacidbutnotProline(Baiet.al.,2019).Inaddition,thisenzymecomplexisalsopartoftheglycosyltransferase-C(GT-C)fold,whichisaproteinthathasatransmembranehelicaldomainandamixofα/βsolubledomains(BaiandLi2019).Onthispage,thestructureoftheOST-Aanditscomponents;itsmechanism,anddiseasesassociatedwiththiscomplexarediscussed.==Structure====ActiveSite====Function====Disease==ThisisasamplescenecreatedwithSATto<scenename="/12/3456/Sample/1">color</scene>byGroup,andanothertomake<scenename="/12/3456/Sample/2">atransparentrepresentation</scene>oftheprotein.YoucanmakeyourownscenesonSATstartingfromscratchorloadingandeditingoneofthesesamplescenes.</li></ol></ref>