Structural highlights
Publication Abstract from PubMedThe 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 x 0.02 x 1 mm. The crystals belonged to the space group P3221 with unit-cell parameters of a = b = 136 A, c = 55.0 A. 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 A 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. Crystal structure of endo-1,4-beta-glucanase from Eisenia fetida.,Arimori T, Ito A, Nakazawa M, Ueda M, Tamada T J Synchrotron Radiat. 2013 Nov;20(Pt 6):884-9. doi: 10.1107/S0909049513021110., Epub 2013 Oct 1. PMID:24121333[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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