1XYO

STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI

1XYO の概要

• エントリーDOI: 10.2210/pdb1xyo/pdb
• 分子名称: ENDO-1,4-BETA-XYLANASE II (2 entities in total)
• 機能のキーワード: xylanase, hydrolase
• 由来する生物種: Hypocrea jecorina
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41676.87

構造登録者

Rouvinen, J.,Torronen, A. (登録日: 1994-08-09, 公開日: 1995-08-08, 最終更新日: 2024-10-23)

主引用文献

Torronen, A.,Rouvinen, J.
Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei.
Biochemistry, 34:847-856, 1995

PubMed Abstract: Three-dimensional structures of two major endo-1,4-xylanases, XYNI and XYNII from Trichoderma reesei, have been determined by X-ray crystallography. The amino acid sequences of both enzymes are highly homologous (identity approximately 50%), and both XYNI and XYNII exist as a single domain that contains two mostly antiparallel beta-sheets which are packed against each other. The beta-sheet structure is twisted, forming a cleft where the active site is situated. Two glutamic acids in the cleft, Glu75 and Glu164 in XYNI as well as Glu86 and Glu177 in XYNII, are most likely involved in catalysis. Inspection of the structures reveals that the width of the active site cleft and the number of subsites are different in XYNI and XYNII. The active site is narrower in XYNI and probably contains only three subsites, whereas the number of subsites in XYNII is most likely five. Variations in the surroundings of catalytic residue Glu164XYNI/Glu177XYNII are thought to explain the pH optimum differences observed in XYNI and XYNII.

PubMed: 7827044
DOI: 10.1021/bi00003a019

実験手法

X-RAY DIFFRACTION (1.5 Å)