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Crystal structure of endo-1,4-$$beta$$-glucanase from ${it Eisenia foetida}$

Arimori, Takao*; Ito, Akihiro*; Nakazawa, Masami*; Ueda, Mitsuhiro*; Tamada, Taro

The saccharification process is essential for bioethanol production from woody biomass including celluloses. Cold-adapted cellulase, which has sufficient activity at low temperature ($$<$$ 293 K), is capable of reducing heating costs during the saccharification process and is suitable for simultaneous saccharification and fermentation. Endo-1,4-$$beta$$-glucanase from the earthworm Eisenia fetida (EF-EG2) belonging to glycoside hydrolase family 9 has been shown to have the highest activity at 313 K, and also retained a comparatively high activity at 283 K. The recombinant EF-EG2 was purified expressed in Pichia pastoris, and then grew needle-shaped crystals with dimensions of 0.02 $$times$$ 0.02 $$times$$ 1 mm. The crystals belonged to the space group P3221 with unit-cell parameters of $$a$$ = $$b$$ =136 ${AA}$, $$c$$ = 55.0 ${AA}$,. The final model of EF-EG2, including 435 residues, two ions, seven crystallization reagents and 696 waters, was refined to a crystallographic $$R$$-factor of 14.7% (free $$R$$-factor of 16.8%) to 1.5 ${AA}$, resolution. The overall structure of EF-EG2 has an ($$alpha$$/$$alpha$$)$$_{6}$$ barrel fold which contains a putative active-site cleft and a negatively charged surface. This structural information helps us understand the catalytic and cold adaptation mechanisms of EF-EG2.

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