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2OVW

ENDOGLUCANASE I COMPLEXED WITH CELLOBIOSE

Summary for 2OVW
Entry DOI10.2210/pdb2ovw/pdb
Related PRD IDPRD_900005
DescriptorENDOGLUCANASE I, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsglycosyl hydrolase, endoglucanase i, complexed with cellobiose, glycosylated protein, hydrolase
Biological sourceFusarium oxysporum
Total number of polymer chains4
Total formula weight181880.13
Authors
Sulzenbacher, G.,Davies, G.J.,Schulein, M. (deposition date: 1997-04-04, release date: 1998-04-08, Last modification date: 2024-10-16)
Primary citationSulzenbacher, G.,Schulein, M.,Davies, G.J.
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, 1997
Cited by
PubMed 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.
PubMed: 9153432
DOI: 10.1021/bi962963+
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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