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2ovw
From Proteopedia
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| - | [[Image:2ovw.gif|left|200px]]<br /> | + | [[Image:2ovw.gif|left|200px]]<br /><applet load="2ovw" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ovw" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2ovw, resolution 2.3Å" /> | caption="2ovw, resolution 2.3Å" /> | ||
'''ENDOGLUCANASE I COMPLEXED WITH CELLOBIOSE'''<br /> | '''ENDOGLUCANASE I COMPLEXED WITH CELLOBIOSE'''<br /> | ||
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==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] | + | 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] Known structural/functional Sites: <scene name='pdbsite=CTA:Catalytic Residues'>CTA</scene>, <scene name='pdbsite=CTB:Catalytic Residues'>CTB</scene>, <scene name='pdbsite=CTC:Catalytic Residues'>CTC</scene> and <scene name='pdbsite=CTD:Catalytic Residues'>CTD</scene>. 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]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 20:13:24 2007'' |
Revision as of 18:03, 18 December 2007
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ENDOGLUCANASE I COMPLEXED WITH 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
2OVW is a Single protein structure of sequence from Fusarium oxysporum with NAG and CBI as ligands. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Sites: , , and . 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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