Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.5/7135
Título: Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure
Autor: 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
Palavras-chave: Cell-surface Enzymes
Protein Complexes
Protein Dynamics
Structural Biology
Modular Assembly
Small Angle X-ray Scattering
Data: 22-Jan-2013
Editora: The American Society for Biochemistry and Molecular Biology
Citação: 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
Resumo: Clostridium 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.
Descrição: Articles in International Journals
Peer review: yes
URI: http://hdl.handle.net/10400.5/7135
DOI: 10.1074/jbc.M112.408757
ISSN: 1083-351X (online)
Versão do Editor: http://www.jbc.org/content/288/11/7978
Aparece nas colecções:DPASA - Artigos de revista
CIISA - Artigos em revistas internacionais

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