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

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 re...

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Autores principales:	Olson, L.J., Orsi, R., Alculumbre, S.G., Peterson, F.C., Stigliano, I.D., Parodi, A.J., D'Alessio, C., Dahms, N.M.
Formato:	JOUR
Materias:	Binding pockets Conserved residues Endoplasmic reticulum Enzymatic activities Glucose residues Glucosyltransferases Nascent protein Three-dimensional structure Cell membranes Glucose Glycoproteins Nuclear magnetic resonance spectroscopy Trimming Proteins alpha glucosidase ab glucosidase glucosidase II alpha glucosidase II beta glycan glycoprotein glycosidase lectin mannose mannose 6 phosphatase receptor homology n glycan somatomedin B receptor unclassified drug uridine diphosphate article binding affinity binding site carboxy terminal sequence controlled study endoplasmic reticulum enzyme active site enzyme activity enzyme assay enzyme localization enzyme regulation Escherichia coli in vivo study molecular dynamics nonhuman nuclear magnetic resonance spectroscopy priority journal protein binding protein domain protein expression protein folding protein protein interaction quality control residue analysis Schizosaccharomyces pombe Endoplasmic Reticulum (ER) Glucosidase II β Glycobiology Glycoprotein MRH Domain N-Glycan NMR Structural Biology alpha-Glucosidases Crystallography, X-Ray Endoplasmic Reticulum Mannose Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Schizosaccharomyces Schizosaccharomyces pombe Proteins
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00219258_v288_n23_p16460_Olson
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_00219258_v288_n23_p16460_Olson2023-10-03T14:23:19Z 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 Olson, L.J. Orsi, R. Alculumbre, S.G. Peterson, F.C. Stigliano, I.D. Parodi, A.J. D'Alessio, C. Dahms, N.M. Binding pockets Conserved residues Endoplasmic reticulum Enzymatic activities Glucose residues Glucosyltransferases Nascent protein Three-dimensional structure Cell membranes Glucose Glycoproteins Nuclear magnetic resonance spectroscopy Trimming Proteins alpha glucosidase ab glucosidase glucosidase II alpha glucosidase II beta glycan glycoprotein glycosidase lectin mannose mannose 6 phosphatase receptor homology n glycan somatomedin B receptor unclassified drug uridine diphosphate article binding affinity binding site carboxy terminal sequence controlled study endoplasmic reticulum enzyme active site enzyme activity enzyme assay enzyme localization enzyme regulation Escherichia coli in vivo study molecular dynamics nonhuman nuclear magnetic resonance spectroscopy priority journal protein binding protein domain protein expression protein folding protein protein interaction quality control residue analysis Schizosaccharomyces pombe Endoplasmic Reticulum (ER) Glucosidase II β Glycobiology Glycoprotein MRH Domain N-Glycan NMR Structural Biology alpha-Glucosidases Crystallography, X-Ray Endoplasmic Reticulum Glycoproteins Mannose Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Schizosaccharomyces Schizosaccharomyces pombe Proteins 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 GIIβ 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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219258_v288_n23_p16460_Olson
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Binding pockets Conserved residues Endoplasmic reticulum Enzymatic activities Glucose residues Glucosyltransferases Nascent protein Three-dimensional structure Cell membranes Glucose Glycoproteins Nuclear magnetic resonance spectroscopy Trimming Proteins alpha glucosidase ab glucosidase glucosidase II alpha glucosidase II beta glycan glycoprotein glycosidase lectin mannose mannose 6 phosphatase receptor homology n glycan somatomedin B receptor unclassified drug uridine diphosphate article binding affinity binding site carboxy terminal sequence controlled study endoplasmic reticulum enzyme active site enzyme activity enzyme assay enzyme localization enzyme regulation Escherichia coli in vivo study molecular dynamics nonhuman nuclear magnetic resonance spectroscopy priority journal protein binding protein domain protein expression protein folding protein protein interaction quality control residue analysis Schizosaccharomyces pombe Endoplasmic Reticulum (ER) Glucosidase II β Glycobiology Glycoprotein MRH Domain N-Glycan NMR Structural Biology alpha-Glucosidases Crystallography, X-Ray Endoplasmic Reticulum Glycoproteins Mannose Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Schizosaccharomyces Schizosaccharomyces pombe Proteins
spellingShingle	Binding pockets Conserved residues Endoplasmic reticulum Enzymatic activities Glucose residues Glucosyltransferases Nascent protein Three-dimensional structure Cell membranes Glucose Glycoproteins Nuclear magnetic resonance spectroscopy Trimming Proteins alpha glucosidase ab glucosidase glucosidase II alpha glucosidase II beta glycan glycoprotein glycosidase lectin mannose mannose 6 phosphatase receptor homology n glycan somatomedin B receptor unclassified drug uridine diphosphate article binding affinity binding site carboxy terminal sequence controlled study endoplasmic reticulum enzyme active site enzyme activity enzyme assay enzyme localization enzyme regulation Escherichia coli in vivo study molecular dynamics nonhuman nuclear magnetic resonance spectroscopy priority journal protein binding protein domain protein expression protein folding protein protein interaction quality control residue analysis Schizosaccharomyces pombe Endoplasmic Reticulum (ER) Glucosidase II β Glycobiology Glycoprotein MRH Domain N-Glycan NMR Structural Biology alpha-Glucosidases Crystallography, X-Ray Endoplasmic Reticulum Glycoproteins Mannose Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Schizosaccharomyces Schizosaccharomyces pombe Proteins 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
topic_facet	Binding pockets Conserved residues Endoplasmic reticulum Enzymatic activities Glucose residues Glucosyltransferases Nascent protein Three-dimensional structure Cell membranes Glucose Glycoproteins Nuclear magnetic resonance spectroscopy Trimming Proteins alpha glucosidase ab glucosidase glucosidase II alpha glucosidase II beta glycan glycoprotein glycosidase lectin mannose mannose 6 phosphatase receptor homology n glycan somatomedin B receptor unclassified drug uridine diphosphate article binding affinity binding site carboxy terminal sequence controlled study endoplasmic reticulum enzyme active site enzyme activity enzyme assay enzyme localization enzyme regulation Escherichia coli in vivo study molecular dynamics nonhuman nuclear magnetic resonance spectroscopy priority journal protein binding protein domain protein expression protein folding protein protein interaction quality control residue analysis Schizosaccharomyces pombe Endoplasmic Reticulum (ER) Glucosidase II β Glycobiology Glycoprotein MRH Domain N-Glycan NMR Structural Biology alpha-Glucosidases Crystallography, X-Ray Endoplasmic Reticulum Glycoproteins Mannose Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Schizosaccharomyces Schizosaccharomyces pombe Proteins
description	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 GIIβ 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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
format	JOUR
author	Olson, L.J. Orsi, R. Alculumbre, S.G. Peterson, F.C. Stigliano, I.D. Parodi, A.J. D'Alessio, C. Dahms, N.M.
author_facet	Olson, L.J. Orsi, R. Alculumbre, S.G. Peterson, F.C. Stigliano, I.D. Parodi, A.J. D'Alessio, C. Dahms, N.M.
author_sort	Olson, L.J.
title	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
title_short	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
title_full	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
title_fullStr	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
title_full_unstemmed	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
title_sort	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
url	http://hdl.handle.net/20.500.12110/paper_00219258_v288_n23_p16460_Olson
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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

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