2LVX
MRH domain of the Glucosidase II beta subunit from S. pombe
Summary for 2LVX
| Entry DOI | 10.2210/pdb2lvx/pdb |
| NMR Information | BMRB: 18592 |
| Descriptor | Glucosidase 2 subunit beta (1 entity in total) |
| Functional Keywords | mrh domain, lectin, glycobiology, protein folding, hydrolase, sugar binding protein |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Cellular location | Endoplasmic reticulum: Q9USH8 |
| Total number of polymer chains | 1 |
| Total formula weight | 10543.98 |
| Authors | Dahms, N.M.,Olson, L.J.,Peterson, F.C. (deposition date: 2012-07-12, release date: 2013-05-01, Last modification date: 2024-10-09) |
| Primary citation | 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 Cited by 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: 23609449DOI: 10.1074/jbc.M113.450239 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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