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• W3120067553 endingPage "850" @default.
• W3120067553 startingPage "838" @default.
• W3120067553 abstract "Asparagine-linked glycosylation, also known as N-linked glycosylation, is an essential and highly conserved co- and post-translational protein modification in eukaryotes and some prokaryotes. In the central step of this reaction, a carbohydrate moiety is transferred from a lipid-linked donor to the side-chain of a consensus asparagine in a nascent protein as it is synthesized at the ribosome. Complete loss of oligosaccharyltransferase (OST) function is lethal in eukaryotes. This reaction is carried out by a membrane-associated multisubunit enzyme, OST, localized in the endoplasmic reticulum. The smallest subunit, Ost4, contains a single membrane-spanning helix that is critical for maintaining the stability and activity of OST. Mutation of any residue from Met18 to Ile24 of Ost4 destabilizes the enzyme complex, affecting its activity. Here, we report solution nuclear magnetic resonance structures and molecular dynamics (MD) simulations of Ost4 and Ost4V23D in micelles. Our studies revealed that while the point mutation did not impact the structure of the protein, it affected its position and solvent exposure in the membrane mimetic environment. Furthermore, our MD simulations of the membrane-bound OST complex containing either WT or V23D mutant demonstrated disruption of most hydrophobic helix-helix interactions between Ost4V23D and transmembrane TM12 and TM13 of Stt3. This disengagement of Ost4V23D from the OST complex led to solvent exposure of the D23 residue in the hydrophobic pocket created by these interactions. Our study not only solves the structures of yeast Ost4 subunit and its mutant but also provides a basis for the destabilization of the OST complex and reduced OST activity." @default.
• W3120067553 created "2021-01-18" @default.
• W3120067553 creator A5068534341 @default.
• W3120067553 creator A5079209474 @default.
• W3120067553 creator A5082496642 @default.
• W3120067553 creator A5091239193 @default.
• W3120067553 date "2021-01-12" @default.
• W3120067553 modified "2023-10-16" @default.
• W3120067553 title "NMR and MD simulations reveal the impact of the V23D mutation on the function of yeast oligosaccharyltransferase subunit Ost4" @default.
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• W3120067553 doi "https://doi.org/10.1093/glycob/cwab002" @default.
• W3120067553 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33442744" @default.
• W3120067553 hasPublicationYear "2021" @default.
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