
pmid: 15781470
The highly conserved membrane protein STT3 is part of the oligosaccharyl transferase complex in the endoplasmic reticulum of eukaryotic cells. Various experimental observations strongly suggest that STT3 contains the active site of the complex. Here, we report a detailed topology study of STT3 from two different organisms, Saccharomyces cerevisiae and mouse, using in vivo and in vitro topology mapping assays. Our results suggest that STT3 has 11 transmembrane helices and an overall N(cyt)-C(lum) orientation.
Models, Molecular, Binding Sites, Glycosylation, Saccharomyces cerevisiae Proteins, beta-Fructofuranosidase, Recombinant Fusion Proteins, Blotting, Western, Cell Membrane, Membrane Proteins, Saccharomyces cerevisiae, Peptide Fragments, Protein Structure, Secondary, Recombinant Proteins, Mice, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Hexosyltransferases, Mutagenesis, Site-Directed, Animals, Electrophoresis, Polyacrylamide Gel, Cloning, Molecular
Models, Molecular, Binding Sites, Glycosylation, Saccharomyces cerevisiae Proteins, beta-Fructofuranosidase, Recombinant Fusion Proteins, Blotting, Western, Cell Membrane, Membrane Proteins, Saccharomyces cerevisiae, Peptide Fragments, Protein Structure, Secondary, Recombinant Proteins, Mice, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Hexosyltransferases, Mutagenesis, Site-Directed, Animals, Electrophoresis, Polyacrylamide Gel, Cloning, Molecular
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