1ree
From Proteopedia
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[[Image:1ree.gif|left|200px]] | [[Image:1ree.gif|left|200px]] | ||
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'''ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE''' | '''ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE''' | ||
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[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
[[Category: Torronen, A.]] | [[Category: Torronen, A.]] | ||
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Xylan degradation]] |
- | [[Category: | + | [[Category: Xylanase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:23:44 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 04:23, 3 May 2008
ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE
Overview
The three-dimensional structures of endo-1,4-xylanase II (XYNII) from Trichoderma reesei complexed with 4,5-epoxypentyl beta-D-xyloside (X-O-C5),3,4-epoxybutyl beta-D-xyloside (X-O-C4), and 2,3-epoxypropyl beta-D-xyloside (X-O-C3) were determined by X-ray crystallography. High-resolution measurement revealed clear electron densities for each ligand. Both X-O-C5 and X-O-C3 were found to form a covalent bond with the putative nucleophile Glu86. Unexpectedly, X-O-C4 was found to bind to the putative acid/base catalyst Glu177. In all three complexes, clear conformational changes were found in XYNII compared to the native structure. These changes were largest in the X-O-C3 complex structure.
About this Structure
1REE is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.
Reference
Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei., Havukainen R, Torronen A, Laitinen T, Rouvinen J, Biochemistry. 1996 Jul 23;35(29):9617-24. PMID:8755744 Page seeded by OCA on Sat May 3 07:23:44 2008