Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.5/7135 |
Resumo: | Articles in International Journals |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structureCell-surface EnzymesCellulaseProtein ComplexesProtein DynamicsStructural BiologyCellulosomeModular AssemblyScaffoldinSmall Angle X-ray ScatteringArticles in International JournalsClostridium thermocellum produces the prototypical cellulosome, a large multienzyme complex that efficiently hydrolyzes plant cell wall polysaccharides into fermentable sugars. This ability has garnered great interest in its potential application in biofuel production. The core non-catalytic scaffoldin subunit, CipA, bears nine type I cohesin modules that interact with the type I dockerin modules of secreted hydrolytic enzymes and promotes catalytic synergy. Because the large size and flexibility of the cellulosome preclude structural determination by traditional means, the structural basis of this synergy remains unclear. Small angle x-ray scattering has been successfully applied to the study of flexible proteins. Here, we used small angle x-ray scattering to determine the solution structure and to analyze the conformational flexibility of two overlapping N-terminal cellulosomal scaffoldin fragments comprising two type I cohesin modules and the cellulose-specific carbohydrate-binding module from CipA in complex with Cel8A cellulases. The pair distribution functions, ab initio envelopes, and rigid body models generated for these two complexes reveal extended structures. These two N-terminal cellulosomal fragments are highly dynamic and display no preference for extended or compact conformations. Overall, our work reveals structural and dynamic features of the N terminus of the CipA scaffoldin that may aid in cellulosome substrate recognition and binding.The American Society for Biochemistry and Molecular BiologyRepositório da Universidade de LisboaCurrie, Mark A.Cameron, KateDias, Fernando M. V.Spencer, Holly L.Bayer, Edward A.Fontes, Carlos M. G. A.Smith, Steven P.Jia, Zongchao2014-09-10T13:18:58Z2013-01-222013-01-22T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.5/7135engCurrie, M.A., et al. (2013). Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure. Journal of Biological Chemistry, 288(11), 7978-7985. doi: 10.1074/jbc.M112.4087571083-351X (online)10.1074/jbc.M112.408757info: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:RCAAP2023-03-06T14:37:53Zoai:www.repository.utl.pt:10400.5/7135Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:54:20.198240Repositório 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 |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
title |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
spellingShingle |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure Currie, Mark A. Cell-surface Enzymes Cellulase Protein Complexes Protein Dynamics Structural Biology Cellulosome Modular Assembly Scaffoldin Small Angle X-ray Scattering |
title_short |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
title_full |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
title_fullStr |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
title_full_unstemmed |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
title_sort |
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure |
author |
Currie, Mark A. |
author_facet |
Currie, Mark A. Cameron, Kate Dias, Fernando M. V. Spencer, Holly L. Bayer, Edward A. Fontes, Carlos M. G. A. Smith, Steven P. Jia, Zongchao |
author_role |
author |
author2 |
Cameron, Kate Dias, Fernando M. V. Spencer, Holly L. Bayer, Edward A. Fontes, Carlos M. G. A. Smith, Steven P. Jia, Zongchao |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Repositório da Universidade de Lisboa |
dc.contributor.author.fl_str_mv |
Currie, Mark A. Cameron, Kate Dias, Fernando M. V. Spencer, Holly L. Bayer, Edward A. Fontes, Carlos M. G. A. Smith, Steven P. Jia, Zongchao |
dc.subject.por.fl_str_mv |
Cell-surface Enzymes Cellulase Protein Complexes Protein Dynamics Structural Biology Cellulosome Modular Assembly Scaffoldin Small Angle X-ray Scattering |
topic |
Cell-surface Enzymes Cellulase Protein Complexes Protein Dynamics Structural Biology Cellulosome Modular Assembly Scaffoldin Small Angle X-ray Scattering |
description |
Articles in International Journals |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-01-22 2013-01-22T00:00:00Z 2014-09-10T13:18:58Z |
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 |
http://hdl.handle.net/10400.5/7135 |
url |
http://hdl.handle.net/10400.5/7135 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Currie, M.A., et al. (2013). Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure. Journal of Biological Chemistry, 288(11), 7978-7985. doi: 10.1074/jbc.M112.408757 1083-351X (online) 10.1074/jbc.M112.408757 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
The American Society for Biochemistry and Molecular Biology |
publisher.none.fl_str_mv |
The American Society for Biochemistry and Molecular Biology |
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 |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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 |
repository.mail.fl_str_mv |
|
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1799131019512643584 |