2LVX

MRH domain of the Glucosidase II beta subunit from S. pombe

2LVX の概要

• エントリーDOI: 10.2210/pdb2lvx/pdb
• NMR情報: BMRB: 18592
• 分子名称: Glucosidase 2 subunit beta (1 entity in total)
• 機能のキーワード: mrh domain, lectin, glycobiology, protein folding, hydrolase, sugar binding protein
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• 細胞内の位置: Endoplasmic reticulum: Q9USH8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10543.98

構造登録者

Dahms, N.M.,Olson, L.J.,Peterson, F.C. (登録日: 2012-07-12, 公開日: 2013-05-01, 最終更新日: 2024-10-09)

主引用文献

Olson, L.J.,Orsi, R.,Alculumbre, S.G.,Peterson, F.C.,Stigliano, I.D.,Parodi, A.J.,D'Alessio, C.,Dahms, N.M.
Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum.
J.Biol.Chem., 288:16460-16475, 2013

PubMed Abstract: Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein folding in the endoplasmic reticulum. GII removes the two innermost glucose residues from the Glc3Man9GlcNAc2 transferred to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase. GII is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit. GIIβ participates in the endoplasmic reticulum localization of GIIα and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GIIβ MRH domain by NMR spectroscopy. It adopts a β-barrel fold similar to that of other MRH domains, but its binding pocket is the most shallow known to date as it accommodates a single mannose residue. In addition, we identified a conserved residue outside the binding pocket (Trp-409) present in GIIβ but not in other MRHs that influences GII glucose trimming activity.

PubMed: 23609449
DOI: 10.1074/jbc.M113.450239

実験手法

SOLUTION NMR