2ovw: Difference between revisions

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==Overview==
==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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9153432 (full description)]]
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==
==About this Structure==
2OVW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]] with NAG and CBI as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Cellulase Cellulase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]]. Structure known Active Sites: CTA, CTB, CTC and CTD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OVW OCA]].  
2OVW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with NAG and CBI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Structure known Active Sites: CTA, CTB, CTC and CTD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OVW OCA].  


==Reference==
==Reference==
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[[Category: glycosylated protein]]
[[Category: glycosylated protein]]


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