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

Bibliographic Details
Main Author: Currie, Mark A.
Publication Date: 2013
Other Authors: Cameron, Kate, Dias, Fernando M. V., Spencer, Holly L., Bayer, Edward A., Fontes, Carlos M. G. A., Smith, Steven P., Jia, Zongchao
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/10400.5/7135
Summary: 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:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-03-17T15:23:41Zoai:repositorio.ulisboa.pt:10400.5/7135Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T03:41:54.167693Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
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:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron:RCAAP
instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
institution RCAAP
reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
_version_ 1833601800962310144

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