2ovw
From Proteopedia
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|PDB= 2ovw |SIZE=350|CAPTION= <scene name='initialview01'>2ovw</scene>, resolution 2.3Å | |PDB= 2ovw |SIZE=350|CAPTION= <scene name='initialview01'>2ovw</scene>, resolution 2.3Å | ||
|SITE= <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> | |SITE= <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> | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ovw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovw OCA], [http://www.ebi.ac.uk/pdbsum/2ovw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ovw RCSB]</span> | ||
}} | }} | ||
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[[Category: Schulein, M.]] | [[Category: Schulein, M.]] | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
| - | [[Category: CBI]] | ||
| - | [[Category: NAG]] | ||
[[Category: complexed with cellobiose]] | [[Category: complexed with cellobiose]] | ||
[[Category: endoglucanase i]] | [[Category: endoglucanase i]] | ||
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[[Category: glycosylated protein]] | [[Category: glycosylated protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:55 2008'' |
Revision as of 01:23, 31 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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