This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1red
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1red" size="450" color="white" frame="true" align="right" spinBox="true" caption="1red, resolution 1.6Å" /> '''ENDO-1,4-BETA-XYLANAS...)
Next diff →
Revision as of 23:24, 20 November 2007
|
ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 4,5-EPOXYPENTYL-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
1RED is a Single protein structure of sequence from Hypocrea jecorina with C5X 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
Page seeded by OCA on Wed Nov 21 01:31:19 2007
