1ree
From Proteopedia
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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 with C4X and BEZ as ligands. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 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
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