Part:BBa_K2804005

CBD cipA fused to sfGFP under the control of LacI promoter

Usage and Biology

Cellulose binding domains (CBDs) have been widely used in scientific research for their biotechnological applications. Originaly, they are part of the more efficient cellulases improving the binding of the catalytic domain. In this part, the CBD of the scaffolding protein cipA of one of the most efficient cellulolityc bacteria, "Clostridium thermocellum", is fused to sfGFP with a 6X Histidine tail in order to visualize and measure at single-molecule level the interaction between the CBD cipA and bacterial cellulose.

Figure 1: Tridimensional structure of CBD cipA-sfGFP obtained from the server I-Tasser.

Usage and Biology

Kruus, K., Lua, A. C., Demain, A. L., & Wu, J. H. (1995). The anchorage function of CipA (CelL), a scaffolding protein of the Clostridium thermocellum cellulosome. Proceedings of the National Academy of Sciences of the United States of America, 92(20), 9254–9258.

Figure 1: Schematic overview of the enhancement mechanism of electron shuttle-mediated electron transfer between bacteria and the anode of MFCs by the synthetic porin OprF. Oxidized mediators diffuse into the periplasmatic space where they accept electrons. Reduced mediators are secreted through outer membrane porins and donate their electrons to the electrode.

References

Kruus, K., Lua, A. C., Demain, A. L., & Wu, J. H. (1995). The anchorage function of CipA (CelL), a scaffolding protein of the Clostridium thermocellum cellulosome. Proceedings of the National Academy of Sciences of the United States of America, 92(20), 9254–9258.