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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/71438
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:16:03Zoai: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:34982025-09-29 10:16:03.628CONICET 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 |
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1844614102087892992 |
score |
13.070432 |