7E9S

Archaeal oligosaccharyltransferase AglB from Archaeoglobus fulgidus in complex with an inhibitory peptide and a dolichol-phosphate

7E9S の概要

• エントリーDOI: 10.2210/pdb7e9s/pdb
• 分子名称: Dolichyl-phosphooligosaccharide-protein glycotransferase 3, a polypeptide linked to an inhibitory N-glycosylation sequon-containing peptide, MANGANESE (II) ION, ... (7 entities in total)
• 機能のキーワード: protein n-glycosylation, ternary complex, sequon-containing peptide, dolichol-phosphate, transferase
• 由来する生物種: Archaeoglobus fulgidus DSM 4304; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102938.84

構造登録者

Taguchi, Y.,Hirata, K.,Kohda, D. (登録日: 2021-03-05, 公開日: 2021-09-08, 最終更新日: 2024-10-23)

主引用文献

Taguchi, Y.,Yamasaki, T.,Ishikawa, M.,Kawasaki, Y.,Yukimura, R.,Mitani, M.,Hirata, K.,Kohda, D.
The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.
Commun Biol, 4:941-941, 2021

PubMed Abstract: Oligosaccharyltransferase (OST) catalyzes oligosaccharide transfer to the Asn residue in the N-glycosylation sequon, Asn-X-Ser/Thr, where Pro is strictly excluded at position X. Considering the unique structural properties of proline, this exclusion may not be surprising, but the structural basis for the rejection of Pro residues should be explained explicitly. Here we determined the crystal structure of an archaeal OST in a complex with a sequon-containing peptide and dolichol-phosphate to a 2.7 Å resolution. The sequon part in the peptide forms two inter-chain hydrogen bonds with a conserved amino acid motif, TIXE. We confirmed the essential role of the TIXE motif and the adjacent regions by extensive alanine-scanning of the external loop 5. A Ramachandran plot revealed that the ring structure of the Pro side chain is incompatible with the ϕ backbone dihedral angle around -150° in the rigid sequon-TIXE structure. The present structure clearly provides the structural basis for the exclusion of Pro residues from the N-glycosylation sequon.

PubMed: 34354228
DOI: 10.1038/s42003-021-02473-8

実験手法

X-RAY DIFFRACTION (2.7 Å)