Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose

Detalhes bibliográficos
Autor(a) principal: Najmudin, Shabir
Data de Publicação: 2008
Outros Autores: Pinheiro, Benedita A., Romão, Maria J., Prates, José A. M., Fontes, Carlos M. G. A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.1107/S1744309108019696
Resumo: The cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution.
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spelling Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaoseClostridium thermocellumEndo-1,4-β-D-xylanase 10BStructural BiologyBiophysicsBiochemistryGeneticsCondensed Matter PhysicsThe cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution.DQ - Departamento de QuímicaCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)RUNNajmudin, ShabirPinheiro, Benedita A.Romão, Maria J.Prates, José A. M.Fontes, Carlos M. G. A.2019-03-11T23:15:24Z2008-08-182008-08-18T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article4application/pdfhttps://doi.org/10.1107/S1744309108019696eng1744-3091PURE: 12012690http://www.scopus.com/inward/record.url?scp=49249121067&partnerID=8YFLogxKhttps://doi.org/10.1107/S1744309108019696info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:29:46Zoai:run.unl.pt:10362/62997Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:33:50.110764Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
title Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
spellingShingle Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
Najmudin, Shabir
Clostridium thermocellum
Endo-1,4-β-D-xylanase 10B
Structural Biology
Biophysics
Biochemistry
Genetics
Condensed Matter Physics
title_short Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
title_full Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
title_fullStr Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
title_full_unstemmed Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
title_sort Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
author Najmudin, Shabir
author_facet Najmudin, Shabir
Pinheiro, Benedita A.
Romão, Maria J.
Prates, José A. M.
Fontes, Carlos M. G. A.
author_role author
author2 Pinheiro, Benedita A.
Romão, Maria J.
Prates, José A. M.
Fontes, Carlos M. G. A.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv DQ - Departamento de Química
CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)
RUN
dc.contributor.author.fl_str_mv Najmudin, Shabir
Pinheiro, Benedita A.
Romão, Maria J.
Prates, José A. M.
Fontes, Carlos M. G. A.
dc.subject.por.fl_str_mv Clostridium thermocellum
Endo-1,4-β-D-xylanase 10B
Structural Biology
Biophysics
Biochemistry
Genetics
Condensed Matter Physics
topic Clostridium thermocellum
Endo-1,4-β-D-xylanase 10B
Structural Biology
Biophysics
Biochemistry
Genetics
Condensed Matter Physics
description The cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution.
publishDate 2008
dc.date.none.fl_str_mv 2008-08-18
2008-08-18T00:00:00Z
2019-03-11T23:15:24Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1107/S1744309108019696
url https://doi.org/10.1107/S1744309108019696
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1744-3091
PURE: 12012690
http://www.scopus.com/inward/record.url?scp=49249121067&partnerID=8YFLogxK
https://doi.org/10.1107/S1744309108019696
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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