ArticleThe Journal of biological chemistry2013
Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022Article
- Review
- Research progress and the biotechnological applications of multienzyme complex.Applied microbiology and biotechnology · 2021Review
- Cellulosomes: Highly Efficient Cellulolytic Complexes.Sub-cellular biochemistry · 2021Review
- A Biological Nanomachine at Work: Watching the Cellulosome Degrade Crystalline Cellulose.ACS central science · 2020Article
- Dynamic interactions of type I cohesin modules fine-tune the structure of the cellulosome ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- Cellulosomes: bacterial nanomachines for dismantling plant polysaccharides.Nature reviews. Microbiology · 2017Review
- Stoichiometric Assembly of the Cellulosome Generates Maximum Synergy for the Degradation of Crystalline Cellulose, as Revealed by In Vitro Reconstitution of the Clostridium thermocellum Cellulosome.Applied and environmental microbiology · 2015Article
- The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers.The Plant cell · 2014Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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