1RED

ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 4,5-EPOXYPENTYL-BETA-D-XYLOSIDE

Summary for 1RED

• Entry DOI: 10.2210/pdb1red/pdb
• Descriptor: ENDO-1,4-BETA-XYLANASE II, 3-[(2R)-oxiran-2-yl]propyl beta-D-xylopyranoside, BENZOIC ACID, ... (4 entities in total)
• Functional Keywords: xylanase, xylan degradation, hydrolase
• Biological source: Hypocrea jecorina
• Total number of polymer chains: 2
• Total formula weight: 42033.24

Authors

Rouvinen, J.,Havukainen, R.,Torronen, A. (deposition date: 1995-12-21, release date: 1997-01-11, Last modification date: 2020-07-29)

Primary citation

Havukainen, R.,Torronen, A.,Laitinen, T.,Rouvinen, J.
Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei.
Biochemistry, 35:9617-9624, 1996

PubMed Abstract: 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.

PubMed: 8755744
DOI: 10.1021/bi953052n

Experimental method

X-RAY DIFFRACTION (1.6 Å)