3G9B

Crystal structure of reduced Ost6L

3G9B の概要

• エントリーDOI: 10.2210/pdb3g9b/pdb
• 関連するPDBエントリー: 3G7Y
• 分子名称: Dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6 (2 entities in total)
• 機能のキーワード: oxidoreductase, active site loop, redox state, membrane, transferase, transmembrane
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Endoplasmic reticulum membrane; Multi-pass membrane protein (Probable): Q03723
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20342.78

構造登録者

Stirnimann, C.U.,Grimshaw, J.P.A.,Schulz, B.L.,Brozzo, M.S.,Fritsch, F.,Glockshuber, R.,Capitani, G.,Gruetter, M.G.,Aebi, M. (登録日: 2009-02-13, 公開日: 2009-06-16, 最終更新日: 2024-04-03)

主引用文献

Schulz, B.L.,Stirnimann, C.U.,Grimshaw, J.P.,Brozzo, M.S.,Fritsch, F.,Mohorko, E.,Capitani, G.,Glockshuber, R.,Grutter, M.G.,Aebi, M.
Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.
Proc.Natl.Acad.Sci.USA, 106:11061-11066, 2009

PubMed Abstract: Asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. The functions of the protein subunits of oligoasccharyltransferase, apart from the catalytic Stt3p, are ill defined. Here we describe functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p revealed oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state. We found that mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affected the glycosylation efficiency of a subset of glycosylation sites. Our results show that eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding.

PubMed: 19549845
DOI: 10.1073/pnas.0812515106

実験手法

X-RAY DIFFRACTION (1.96 Å)