Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure

Detalhes bibliográficos
Autor(a) principal: Currie, Mark A.
Data de Publicação: 2013
Outros Autores: Cameron, Kate, Dias, Fernando M. V., Spencer, Holly L., Bayer, Edward A., Fontes, Carlos M. G. A., Smith, Steven P., Jia, Zongchao
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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spelling 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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