Abstract
Cellulosomes are highly efficient multienzyme complexes for lignocellulose degradation secreted by some lignocellulolytic bacteria. Cellulosomes are assembled through protein modules named cohesin and dockerin, and multiple cohesin modules in the scaffold protein generally determine the complexity of the cellulosomes. Some cellulosomal proteins contain multiple dockerin modules, which may generate more complex cellulosomal architectures. Genome mining revealed that cellulosomal proteins containing double dockerin modules and a protease module exist in many cellulosome-producing bacteria, and these proteins together with cellulosomal protease inhibitors were proposed to have regulatory roles. However, the structures and functions of these multiple-dockerin proteins in cellulosome have not been reported before. In this paper, we present the NMR chemical shift assignments of the double-dockerin of a cellulosomal protease from Clostridium thermocellum DSM1313. The secondary structures predicted from the chemical shifts agree with the structural arrangement of the tandem dockerin modules. The chemical shift assignments here provide the basis for the structural and functional studies of multiple-dockerin proteins in future.
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Acknowledgements
This work was supported by the National Natural Science Foundation of China (31670735 and 31661143023 to YF, 31800022 to CC, and 31470210 to QC), the “Transformational Technologies for Clean Energy and Demonstration”, Strategic Priority Research Program of the Chinese Academy of Sciences (Grant Number XDA 21060201 to QC), the Shandong Provincial Natural Science Foundation (Grant Number ZR2016CB09 to CC), and the Undergraduate Education and Teaching Reform Research Project of USTB (grant number JG2018M39 to JX).
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Chen, C., Yang, H., Xuan, J. et al. Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum. Biomol NMR Assign 13, 97–101 (2019). https://doi.org/10.1007/s12104-018-9859-7
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DOI: https://doi.org/10.1007/s12104-018-9859-7