PDBsum entry 3wc3

Hydrolase

PDB id: 3wc3

Contents

Protein chain

435 a.a.

Ligands

TRS

FLC

GOL ×5

Metals

_CA

_NA

Waters ×722

PDB id:

3wc3

Name:

Hydrolase

Title:

Crystal structure of endo-1,4-beta-glucanase from eisenia fetida

Structure:

Endo-1, 4-beta-glucanase. Chain: a. Fragment: unp residues 22-456. Engineered: yes

Source:

Eisenia fetida. Brandling worm. Organism_taxid: 6396. Gene: ef-eg2. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

Resolution:

1.50Å R-factor: 0.148 R-free: 0.168

Authors:

T.Arimori,T.Tamada

Key ref:

T.Arimori et al. (2013). Crystal structure of endo-1,4-β-glucanase from Eisenia fetida. J Synchrotron Radiat, 20, 884-889. PubMed id: 24121333 DOI: 10.1107/S0909049513021110

Date:

24-May-13 Release date: 30-Oct-13

Protein chain

I2FI81  (I2FI81_EISFE) -  Endoglucanase from Eisenia fetida

Seq: 456 a.a.

Struc: 435 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.2.1.4 - cellulase.
• Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

DOI no: 10.1107/S0909049513021110

J Synchrotron Radiat 20:884-889 (2013)

PubMed id: 24121333

Crystal structure of endo-1,4-β-glucanase from Eisenia fetida.

T.Arimori, A.Ito, M.Nakazawa, M.Ueda, T.Tamada.

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.