4ovw
From Proteopedia
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ENDOGLUCANASE I COMPLEXED WITH EPOXYBUTYL CELLOBIOSE
Overview
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.
About this Structure
4OVW is a Single protein structure of sequence from Fusarium oxysporum with NAG and IN1 as ligands. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution., Sulzenbacher G, Schulein M, Davies GJ, Biochemistry. 1997 May 13;36(19):5902-11. PMID:9153432
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