8AGC

Structure of yeast oligosaccharylransferase complex with lipid-linked oligosaccharide and non-acceptor peptide bound

8AGC の概要

• エントリーDOI: 10.2210/pdb8agc/pdb
• EMDBエントリー: 15420
• 分子名称: Dolichyl-diphosphooligosaccharide--protein glycotransferase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (18 entities in total)
• 機能のキーワード: n-glycosylation ost complex, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 297648.38

構造登録者

Ramirez, A.S.,de Capitani, M.,Pesciullesi, G.,Kowal, J.,Bloch, J.S.,Irobalieva, R.N.,Aebi, M.,Reymond, J.L.,Locher, K.P. (登録日: 2022-07-19, 公開日: 2022-12-07, 最終更新日: 2025-07-09)

主引用文献

Ramirez, A.S.,de Capitani, M.,Pesciullesi, G.,Kowal, J.,Bloch, J.S.,Irobalieva, R.N.,Reymond, J.L.,Aebi, M.,Locher, K.P.
Molecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase.
Nat Commun, 13:7296-7296, 2022

PubMed Abstract: Oligosaccharyltransferase (OST) is the central enzyme of N-linked protein glycosylation. It catalyzes the transfer of a pre-assembled glycan, GlcNAcManGlc, from a dolichyl-pyrophosphate donor to acceptor sites in secretory proteins in the lumen of the endoplasmic reticulum. Precise recognition of the fully assembled glycan by OST is essential for the subsequent quality control steps of glycoprotein biosynthesis. However, the molecular basis of the OST-donor glycan interaction is unknown. Here we present cryo-EM structures of S. cerevisiae OST in distinct functional states. Our findings reveal that the terminal glucoses (Glc) of a chemo-enzymatically generated donor glycan analog bind to a pocket formed by the non-catalytic subunits WBP1 and OST2. We further find that binding either donor or acceptor substrate leads to distinct primed states of OST, where subsequent binding of the other substrate triggers conformational changes required for catalysis. This alternate priming allows OST to efficiently process closely spaced N-glycosylation sites.

PubMed: 36435935
DOI: 10.1038/s41467-022-35067-x

実験手法

ELECTRON MICROSCOPY (3.1 Å)