3VU1

Crystal structure of the C-terminal globular domain of oligosaccharyltransferase (PhAglB-L, O74088_PYRHO) from Pyrococcus horikoshii

3VU1 の概要

• エントリーDOI: 10.2210/pdb3vu1/pdb
• 関連するPDBエントリー: 3VU0
• 分子名称: Putative uncharacterized protein PH0242, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: glycotransferase, asn-glycosylation, membrane, transferase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115272.27

構造登録者

Nyirenda, J.,Matsumoto, S.,Saitoh, T.,Maita, N.,Noda, N.N.,Inagaki, F.,Kohda, D. (登録日: 2012-06-13, 公開日: 2013-01-23, 最終更新日: 2024-10-30)

主引用文献

Nyirenda, J.,Matsumoto, S.,Saitoh, T.,Maita, N.,Noda, N.N.,Inagaki, F.,Kohda, D.
Crystallographic and NMR Evidence for Flexibility in Oligosaccharyltransferases and Its Catalytic Significance
Structure, 21:32-41, 2013

PubMed Abstract: Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins. It possesses a binding pocket that recognizes Ser and Thr residues at the +2 position in the N-glycosylation consensus, Asn-X-Ser/Thr. We determined the crystal structures of the C-terminal globular domains of the catalytic subunits of two archaeal OSTs. A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects. We characterized its dynamic properties in solution by (15)N NMR relaxation analyses. Intriguingly, the mobile region contains the +2 Ser/Thr-binding pocket. In agreement, the flexibility restriction forced by an engineered disulfide crosslink abolished the enzymatic activity, and its cleavage fully restored activity. These results suggest the necessity of multiple conformational states in the reaction. The dynamic nature of the Ser/Thr pocket could facilitate the efficient scanning of N-glycosylation sequons along nascent polypeptide chains.

PubMed: 23177926
DOI: 10.1016/j.str.2012.10.011

実験手法

X-RAY DIFFRACTION (2.7 Å)