2ovw
From Proteopedia
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- | [[Image:2ovw.gif|left|200px]] | + | [[Image:2ovw.gif|left|200px]] |
- | + | ||
- | '''ENDOGLUCANASE I COMPLEXED WITH CELLOBIOSE''' | + | {{Structure |
+ | |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> | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</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] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''ENDOGLUCANASE I COMPLEXED WITH CELLOBIOSE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2OVW is a [ | + | 2OVW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9153432 9153432] |
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Fusarium oxysporum]] | [[Category: Fusarium oxysporum]] | ||
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[[Category: glycosylated protein]] | [[Category: glycosylated protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:05:11 2008'' |
Revision as of 16:05, 20 March 2008
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, resolution 2.3Å | |||||||
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Sites: | , , and | ||||||
Ligands: | and | ||||||
Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
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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