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PDBsum entry 3wc3
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References listed in PDB file
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Key reference
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Title
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Crystal structure of endo-1,4-β-Glucanase from eisenia fetida.
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Authors
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T.Arimori,
A.Ito,
M.Nakazawa,
M.Ueda,
T.Tamada.
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Ref.
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J Synchrotron Radiat, 2013,
20,
884-889.
[DOI no: ]
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PubMed id
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Abstract
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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.
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