PDBsum entry: 3ovw

Hydrolase

PDB id: 3ovw

Contents

Protein chains

400 a.a. *

Ligands

NAG ×4

Waters ×422

* Residue conservation analysis

PDB id:

3ovw

Name:

Hydrolase

Title:

Endoglucanase i native structure

Structure:

Endoglucanase i. Chain: a, b. Ec: 3.2.1.4

Source:

Fusarium oxysporum. Organism_taxid: 5507

Resolution:

2.30Å R-factor: 0.158 R-free: 0.225

Authors:

G.J.Davies,M.Schulein

Key ref:

G.Sulzenbacher et al. (1997). Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution. Biochemistry, 36, 5902-5911. PubMed id: 9153432 DOI: 10.1021/bi962963+

Date:

06-Oct-97 Release date: 08-Apr-98

Protein chains

P46237  (GUNC_FUSOX) -  Endoglucanase type C

Seq: 429 a.a.

Struc: 400 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.

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (4 terms)
• Biochemical function: hydrolase activity (4 terms)

DOI no: 10.1021/bi962963+

Biochemistry 36:5902-5911 (1997)

PubMed id: 9153432

Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.

G.Sulzenbacher, M.Schülein, G.J.Davies.

ABSTRACT

The mechanisms involved in the enzymatic degradation of cellulose are of great ecological and commercial importance. The breakdown of cellulose by fungal species is performed by a consortium of free enzymes, known as cellobiohydrolases and endoglucanases, which are found in many of the 57 glycosyl hydrolase families. The structure of the endoglucanase I (EG I), found in glycosyl hydrolase family 7, from the thermophilic fungus Fusarium oxysporum has been solved at 2.3 A resolution. In addition to the native enzyme, structures have also been determined with both the affinity label, 3,4-epoxybutyl beta-D-cellobioside, and the reaction product cellobiose. The affinity label is covalently bound, as expected, to the catalytic nucleophile, Glu197, with clear evidence for binding of both the R and S stereoisomers. Cellobiose is found bound to the -2 and -1 subsites of the enzyme. In marked contrast to the structure of EG I with a nonhydrolyzable thiosaccharide analog, which spanned the -2, -1, and +1 subsites and which had a skew-boat conformation for the -1 subsite sugar [Sulzenbacher, G., et al. (1996) Biochemistry 35, 15280-15287], the cellobiose complex shows no pyranoside ring distortion in the -1 subsite, implying that strain is induced primarily by the additional +1 subsite interactions and that the product is found, as expected, in its unstrained conformation.