3WC3
Crystal structure of endo-1,4-beta-glucanase from Eisenia fetida
Summary for 3WC3
| Entry DOI | 10.2210/pdb3wc3/pdb |
| Descriptor | Endo-1, 4-beta-glucanase, CALCIUM ION, SODIUM ION, ... (7 entities in total) |
| Functional Keywords | (alpha/alpha)6 barrel fold, hydrolase, sugar binding |
| Biological source | Eisenia fetida (brandling worm) |
| Total number of polymer chains | 1 |
| Total formula weight | 52279.53 |
| Authors | Arimori, T.,Tamada, T. (deposition date: 2013-05-24, release date: 2013-10-30, Last modification date: 2024-10-09) |
| Primary citation | Arimori, T.,Ito, A.,Nakazawa, M.,Ueda, M.,Tamada, T. Crystal structure of endo-1,4-beta-glucanase from Eisenia fetida J.SYNCHROTRON RADIAT., 20:884-889, 2013 Cited by PubMed Abstract: 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-β-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 × 0.02 × 1 mm. The crystals belonged to the space group P3221 with unit-cell parameters of a = b = 136 Å, c = 55.0 Å. 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 Å resolution. The overall structure of EF-EG2 has an (α/α)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. PubMed: 24121333DOI: 10.1107/S0909049513021110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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