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PDBsum entry 1ree
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-Xylanase ii from trichoderma reesei.
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Authors
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R.Havukainen,
A.Törrönen,
T.Laitinen,
J.Rouvinen.
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Ref.
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Biochemistry, 1996,
35,
9617-9624.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Three-Dimensional structure of endo-1,4-Beta-Xylanase ii from trichoderma reesei: two conformational states in the active site.
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Authors
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A.Törrönen,
A.Harkki,
J.Rouvinen.
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Ref.
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Embo J, 1994,
13,
2493-2501.
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PubMed id
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