Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum

Autores
Olson, Linda J.; Orsi, Ramiro; Alculumbre, Solana G.; Peterson, Francis C.; Stigliano, Ivan Daniel; Parodi, Armando Jose A.; D'alessio, Cecilia; Dahms, Nancy M.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 GII subunit and a regulatory GII subunit. GII participates in the endoplasmic reticulum localization of GII and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GII MRH domain by NMR spectroscopy. It adopts a -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 GII but not in other MRHs that influences GII glucose trimming activity.
Fil: Olson, Linda J.. Medical College Of Wisconsin; Estados Unidos
Fil: Orsi, Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Alculumbre, Solana G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Peterson, Francis C.. Medical College Of Wisconsin; Estados Unidos
Fil: Stigliano, Ivan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Parodi, Armando Jose A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: D'alessio, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Dahms, Nancy M.. Medical College Of Wisconsin; Estados Unidos
Materia
Mrh Domain
Endoplasmic Reticulum
N-Glycan
Glucosidase Ii
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/19644
Acceder
id CONICETDig_a03b21339439fc13fed62fafe83d5720
oai_identifier_str oai:ri.conicet.gov.ar:11336/19644
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic ReticulumOlson, Linda J.Orsi, RamiroAlculumbre, Solana G.Peterson, Francis C.Stigliano, Ivan DanielParodi, Armando Jose A.D'alessio, CeciliaDahms, Nancy M.Mrh DomainEndoplasmic ReticulumN-GlycanGlucosidase Iihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Here 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 GII subunit and a regulatory GII subunit. GII participates in the endoplasmic reticulum localization of GII and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GII MRH domain by NMR spectroscopy. It adopts a -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 GII but not in other MRHs that influences GII glucose trimming activity.Fil: Olson, Linda J.. Medical College Of Wisconsin; Estados UnidosFil: Orsi, Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Alculumbre, Solana G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Peterson, Francis C.. Medical College Of Wisconsin; Estados UnidosFil: Stigliano, Ivan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Parodi, Armando Jose A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: D'alessio, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Dahms, Nancy M.. Medical College Of Wisconsin; Estados UnidosAmerican Society For Biochemistry And Molecular Biology2013-04-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/19644Olson, Linda J.; Orsi, Ramiro; Alculumbre, Solana G.; Peterson, Francis C.; Stigliano, Ivan Daniel; et al.; Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 23; 5-4-2013; 16460-164750021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/288/23/16460.full.html#ref-list-1info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M113.450239info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:10:54Zoai:ri.conicet.gov.ar:11336/19644instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:10:55.069CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
title Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
spellingShingle Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
Olson, Linda J.
Mrh Domain
Endoplasmic Reticulum
N-Glycan
Glucosidase Ii
title_short Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
title_full Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
title_fullStr Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
title_full_unstemmed Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
title_sort Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
dc.creator.none.fl_str_mv Olson, Linda J.
Orsi, Ramiro
Alculumbre, Solana G.
Peterson, Francis C.
Stigliano, Ivan Daniel
Parodi, Armando Jose A.
D'alessio, Cecilia
Dahms, Nancy M.
author Olson, Linda J.
author_facet Olson, Linda J.
Orsi, Ramiro
Alculumbre, Solana G.
Peterson, Francis C.
Stigliano, Ivan Daniel
Parodi, Armando Jose A.
D'alessio, Cecilia
Dahms, Nancy M.
author_role author
author2 Orsi, Ramiro
Alculumbre, Solana G.
Peterson, Francis C.
Stigliano, Ivan Daniel
Parodi, Armando Jose A.
D'alessio, Cecilia
Dahms, Nancy M.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Mrh Domain
Endoplasmic Reticulum
N-Glycan
Glucosidase Ii
topic Mrh Domain
Endoplasmic Reticulum
N-Glycan
Glucosidase Ii
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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 GII subunit and a regulatory GII subunit. GII participates in the endoplasmic reticulum localization of GII and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GII MRH domain by NMR spectroscopy. It adopts a -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 GII but not in other MRHs that influences GII glucose trimming activity.
Fil: Olson, Linda J.. Medical College Of Wisconsin; Estados Unidos
Fil: Orsi, Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Alculumbre, Solana G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Peterson, Francis C.. Medical College Of Wisconsin; Estados Unidos
Fil: Stigliano, Ivan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Parodi, Armando Jose A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: D'alessio, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Dahms, Nancy M.. Medical College Of Wisconsin; Estados Unidos
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 GII subunit and a regulatory GII subunit. GII participates in the endoplasmic reticulum localization of GII and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GII MRH domain by NMR spectroscopy. It adopts a -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 GII but not in other MRHs that influences GII glucose trimming activity.
publishDate 2013
dc.date.none.fl_str_mv 2013-04-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/19644
Olson, Linda J.; Orsi, Ramiro; Alculumbre, Solana G.; Peterson, Francis C.; Stigliano, Ivan Daniel; et al.; Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 23; 5-4-2013; 16460-16475
0021-9258
CONICET Digital
CONICET
url http://hdl.handle.net/11336/19644
identifier_str_mv Olson, Linda J.; Orsi, Ramiro; Alculumbre, Solana G.; Peterson, Francis C.; Stigliano, Ivan Daniel; et al.; Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 23; 5-4-2013; 16460-16475
0021-9258
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/288/23/16460.full.html#ref-list-1
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M113.450239
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842270137118359552
score 13.13397

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