Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate

Autores
Guérin, Diego Marcelo Alejandro; Lascombe, Marie-Bernard; Costabel, Marcelo Daniel; Souchon, Hélène; Lamzin, Victor; Béguin, Pierre; Alzari, Pedro M
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 Å resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat2,5 B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis. © 2002 Elsevier Science Ltd.
Fil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Pasteur; Francia. Hamburg Outstation; Alemania
Fil: Lascombe, Marie-Bernard. Instituto Pasteur; Francia
Fil: Costabel, Marcelo Daniel. Instituto Pasteur; Francia. Hamburg Outstation; Alemania
Fil: Souchon, Hélène. Instituto Pasteur; Francia
Fil: Lamzin, Victor. Hamburg Outstation; Alemania
Fil: Béguin, Pierre. Instituto Pasteur; Francia
Fil: Alzari, Pedro M. Instituto Pasteur; Francia
Materia
ATOMIC RESOLUTION
INVERTING GLYCOSIDASE
PROTEIN-CARBOHYDRATE INTERACTIONS
REACTION MECHANISM
X-RAY CRYSTALLOGRAPHY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/71438
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/71438
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrateGuérin, Diego Marcelo AlejandroLascombe, Marie-BernardCostabel, Marcelo DanielSouchon, HélèneLamzin, VictorBéguin, PierreAlzari, Pedro MATOMIC RESOLUTIONINVERTING GLYCOSIDASEPROTEIN-CARBOHYDRATE INTERACTIONSREACTION MECHANISMX-RAY CRYSTALLOGRAPHYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 Å resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat2,5 B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis. © 2002 Elsevier Science Ltd.Fil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Pasteur; Francia. Hamburg Outstation; AlemaniaFil: Lascombe, Marie-Bernard. Instituto Pasteur; FranciaFil: Costabel, Marcelo Daniel. Instituto Pasteur; Francia. Hamburg Outstation; AlemaniaFil: Souchon, Hélène. Instituto Pasteur; FranciaFil: Lamzin, Victor. Hamburg Outstation; AlemaniaFil: Béguin, Pierre. Instituto Pasteur; FranciaFil: Alzari, Pedro M. Instituto Pasteur; FranciaAcademic Press Ltd - Elsevier Science Ltd2002-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/71438Guérin, Diego Marcelo Alejandro; Lascombe, Marie-Bernard; Costabel, Marcelo Daniel; Souchon, Hélène; Lamzin, Victor; et al.; Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate; Academic Press Ltd - Elsevier Science Ltd; Journal Of Molecular Biology; 316; 5; 5-2002; 1061-10690022-2836CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1006/jmbi.2001.5404info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S002228360195404Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:46:12Zoai:ri.conicet.gov.ar:11336/71438instacron: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:34982025-10-22 11:46:12.4CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
title Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
spellingShingle Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
Guérin, Diego Marcelo Alejandro
ATOMIC RESOLUTION
INVERTING GLYCOSIDASE
PROTEIN-CARBOHYDRATE INTERACTIONS
REACTION MECHANISM
X-RAY CRYSTALLOGRAPHY
title_short Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
title_full Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
title_fullStr Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
title_full_unstemmed Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
title_sort Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate
dc.creator.none.fl_str_mv Guérin, Diego Marcelo Alejandro
Lascombe, Marie-Bernard
Costabel, Marcelo Daniel
Souchon, Hélène
Lamzin, Victor
Béguin, Pierre
Alzari, Pedro M
author Guérin, Diego Marcelo Alejandro
author_facet Guérin, Diego Marcelo Alejandro
Lascombe, Marie-Bernard
Costabel, Marcelo Daniel
Souchon, Hélène
Lamzin, Victor
Béguin, Pierre
Alzari, Pedro M
author_role author
author2 Lascombe, Marie-Bernard
Costabel, Marcelo Daniel
Souchon, Hélène
Lamzin, Victor
Béguin, Pierre
Alzari, Pedro M
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ATOMIC RESOLUTION
INVERTING GLYCOSIDASE
PROTEIN-CARBOHYDRATE INTERACTIONS
REACTION MECHANISM
X-RAY CRYSTALLOGRAPHY
topic ATOMIC RESOLUTION
INVERTING GLYCOSIDASE
PROTEIN-CARBOHYDRATE INTERACTIONS
REACTION MECHANISM
X-RAY CRYSTALLOGRAPHY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 Å resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat2,5 B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis. © 2002 Elsevier Science Ltd.
Fil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Pasteur; Francia. Hamburg Outstation; Alemania
Fil: Lascombe, Marie-Bernard. Instituto Pasteur; Francia
Fil: Costabel, Marcelo Daniel. Instituto Pasteur; Francia. Hamburg Outstation; Alemania
Fil: Souchon, Hélène. Instituto Pasteur; Francia
Fil: Lamzin, Victor. Hamburg Outstation; Alemania
Fil: Béguin, Pierre. Instituto Pasteur; Francia
Fil: Alzari, Pedro M. Instituto Pasteur; Francia
description The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 Å resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat2,5 B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis. © 2002 Elsevier Science Ltd.
publishDate 2002
dc.date.none.fl_str_mv 2002-05
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/11336/71438
Guérin, Diego Marcelo Alejandro; Lascombe, Marie-Bernard; Costabel, Marcelo Daniel; Souchon, Hélène; Lamzin, Victor; et al.; Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate; Academic Press Ltd - Elsevier Science Ltd; Journal Of Molecular Biology; 316; 5; 5-2002; 1061-1069
0022-2836
CONICET Digital
CONICET
url http://hdl.handle.net/11336/71438
identifier_str_mv Guérin, Diego Marcelo Alejandro; Lascombe, Marie-Bernard; Costabel, Marcelo Daniel; Souchon, Hélène; Lamzin, Victor; et al.; Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate; Academic Press Ltd - Elsevier Science Ltd; Journal Of Molecular Biology; 316; 5; 5-2002; 1061-1069
0022-2836
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1006/jmbi.2001.5404
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S002228360195404X
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Ltd - Elsevier Science Ltd
publisher.none.fl_str_mv Academic Press Ltd - Elsevier Science Ltd
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_ 1846782162797330432
score 12.982451

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