2ZAI

Crystal structure of the soluble domain of STT3 from P. furiosus

2ZAI の概要

• エントリーDOI: 10.2210/pdb2zai/pdb
• 関連するPDBエントリー: 2ZAG
• 分子名称: Oligosaccharyl transferase stt3 subunit related protein, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: multi-domain proteins (alpha and beta), transferase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 224206.59

構造登録者

Maita, N. (登録日: 2007-10-05, 公開日: 2007-12-11, 最終更新日: 2024-10-23)

主引用文献

Igura, M.,Maita, N.,Kamishikiryo, J.,Yamada, M.,Obita, T.,Maenaka, K.,Kohda, D.
Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
Embo J., 27:234-243, 2008

PubMed Abstract: Asn-glycosylation is widespread not only in eukaryotes but also in archaea and some eubacteria. Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains. Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner. We also determined the 2.7-A resolution crystal structure of the C-terminal soluble domain of Pyrococcus STT3. The structure-based multiple sequence alignment revealed a new motif, DxxK, which is adjacent to the well-conserved WWDYG motif in the tertiary structure. The mutagenesis of the DK motif residues in yeast STT3 revealed the essential role of the motif in the catalytic activity. The function of this motif may be related to the binding of the pyrophosphate group of lipid-linked oligosaccharide donors through a transiently bound cation. Our structure provides the first structural insights into the formation of the oligosaccharide-asparagine bond.

PubMed: 18046457
DOI: 10.1038/sj.emboj.7601940

実験手法

X-RAY DIFFRACTION (2.7 Å)