The mechanism ofassembly for the enzyme subunits of the natural scaffoldin is not currentlyknown. In our study we focused on the cellulosome-integratingprotein CipA of C. thermocellum and cellulosomal enzymesfrom families 5, 9 and 48. The first coarse-grained model to study theformation and function of the cellulosome assembly was developed within CHARMM.This study aims at understanding the mechanisms involved in the sequentialbinding of the cellulosomal enzymes to the CipA scaffold of C. thermocellum. Understanding thismechanism is essential in order to design efficient engineered cellulosomes. Individual subdomains were also studied with molecular dynamics and normal modeanalysis on cellulose surfaces or with individual cellulose chains. Thesedomains include, catalytic domains, carbohydrate binding domains, fibronectins,as well as the immunoglobulin-like domain. The complex, seven-domain family 9enzyme from C. thermocellum, CbhA, hasbeen extensively studied; several recently determined protein structures haveenabled novel computational studies providing new insights in the role of thisenzyme and the function of its individual subdomains.

Understanding the cellulosome and its assembly: Toward improving consolidated bioprocessing

239th National Meeting (2010)

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