4ovw
From Proteopedia
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- | [[Image:4ovw.jpg|left|200px]] | + | [[Image:4ovw.jpg|left|200px]] |
- | + | ||
- | '''ENDOGLUCANASE I COMPLEXED WITH EPOXYBUTYL CELLOBIOSE''' | + | {{Structure |
+ | |PDB= 4ovw |SIZE=350|CAPTION= <scene name='initialview01'>4ovw</scene>, resolution 2.3Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=IN1:PROPIONIC ACID 2,2-DIHYDROXY-3-(1-GLUCOPYRANOSYLOXY)-METHYLPROPYL ESTER'>IN1</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 EPOXYBUTYL CELLOBIOSE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 4OVW is a [ | + | 4OVW 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=4OVW 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 19:10:30 2008'' |
Revision as of 17:10, 20 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | and | ||||||
Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ENDOGLUCANASE I COMPLEXED WITH EPOXYBUTYL 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
4OVW 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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