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

2013-01-22Journal article Open access
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dc.contributor.authorCurrie, Mark A.
dc.contributor.authorCameron, Kate
dc.contributor.authorDias, Fernando M. V.
dc.contributor.authorSpencer, Holly L.
dc.contributor.authorBayer, Edward A.
dc.contributor.authorFontes, Carlos M. G. A.
dc.contributor.authorSmith, Steven P.
dc.contributor.authorJia, Zongchao
dc.date.accessioned2014-09-10T13:18:58Z
dc.date.available2014-09-10T13:18:58Z
dc.date.issued2013-01-22
dc.descriptionArticles in International Journalspor
dc.description.abstractClostridium 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.por
dc.identifier.citationCurrie, 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.M112.408757por
dc.identifier.doi10.1074/jbc.M112.408757
dc.identifier.issn1083-351X (online)
dc.identifier.urihttp://hdl.handle.net/10400.5/7135
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherThe American Society for Biochemistry and Molecular Biologypor
dc.relation.publisherversionhttp://www.jbc.org/content/288/11/7978por
dc.subjectCell-surface Enzymespor
dc.subjectCellulasepor
dc.subjectProtein Complexespor
dc.subjectProtein Dynamicspor
dc.subjectStructural Biologypor
dc.subjectCellulosomepor
dc.subjectModular Assemblypor
dc.subjectScaffoldinpor
dc.subjectSmall Angle X-ray Scatteringpor
dc.titleSmall angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structurepor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage7985por
oaire.citation.issue11
oaire.citation.startPage7978por
oaire.citation.titleJournal of Biological Chemistrypor
oaire.citation.volume288por
rcaap.rightsopenAccesspor
rcaap.typearticlepor

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