1BG4

XYLANASE FROM PENICILLIUM SIMPLICISSIMUM

1BG4 の概要

• エントリーDOI: 10.2210/pdb1bg4/pdb
• 分子名称: ENDO-1,4-BETA-XYLANASE, SODIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• 機能のキーワード: family 10 xylanase, penicillium simplicissimum, tim-barrel, glycosyl hydrolase
• 由来する生物種: Penicillium simplicissimum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33593.36

構造登録者

Schmidt, A.,Kratky, C. (登録日: 1998-06-05, 公開日: 1998-08-12, 最終更新日: 2024-10-30)

主引用文献

Schmidt, A.,Schlacher, A.,Steiner, W.,Schwab, H.,Kratky, C.
Structure of the xylanase from Penicillium simplicissimum.
Protein Sci., 7:2081-2088, 1998

PubMed Abstract: Despite its relatively low pH and temperature optimum, the xylanase from Penicillium simplicissimum performs exceedingly well under conditions of paper bleaching. We have purified and characterized this enzyme, which belongs to family 10 of glycosyl hydrolases. Its gene was cloned, and the sequence of the protein was deduced from the nucleotide sequence. The xylanase was crystallized from ammonium sulfate at pH 8.4, and X-ray data were collected at cryo-temperature to a crystallographic resolution of 1.75 A. The crystal structure was solved by molecular replacement using the catalytic domain of the Clostridium thermocellum xylanase as a search model, and refined to a residual of R = 20% (R(free) = 23%) for data between 10 and 1.75 A. The xylanase folds in an (alpha/beta)8 barrel (TIM-barrel), with additional helices and loops arranged at the "top" forming the active site cleft. In its overall shape, the P. simplicissimum xylanase structure is similar to other family 10 xylanases, but its active site cleft is much shallower and wider. This probably accounts for the differences in catalysis and in the mode of action of this enzyme. Three glycerol molecules were observed to bind within the active site groove, one of which interacts directly with the catalytic glutamate residues. It appears that they occupy putative xylose binding subsites.

PubMed: 9792094

実験手法

X-RAY DIFFRACTION (1.75 Å)