3NJ3

Crystal structure of xylanase 10B from Thermotoga petrophila RKU-1 in complex with xylobiose

3NJ3 の概要

• エントリーDOI: 10.2210/pdb3nj3/pdb
• 関連するPDBエントリー: 3NIY
• 関連するBIRD辞書のPRD_ID: PRD_900116
• 分子名称: Endo-1,4-beta-xylanase, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: tim barrel, xylanase, hydrolase
• 由来する生物種: Thermotoga petrophila RKU-1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81914.28

構造登録者

Santos, C.R.,Meza, A.N.,Trindade, D.M.,Ruller, R.,Squina, F.M.,Prade, R.A.,Murakami, M.T. (登録日: 2010-06-16, 公開日: 2011-05-04, 最終更新日: 2024-02-21)

主引用文献

Santos, C.R.,Meza, A.N.,Hoffmam, Z.B.,Silva, J.C.,Alvarez, T.M.,Ruller, R.,Giesel, G.M.,Verli, H.,Squina, F.M.,Prade, R.A.,Murakami, M.T.
Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1.
Biochem.Biophys.Res.Commun., 403:214-219, 2010

PubMed Abstract: Endo-xylanases play a key role in the depolymerization of xylan and recently, they have attracted much attention owing to their potential applications on biofuels and paper industries. In this work, we have investigated the molecular basis for the action mode of xylanases 10B at high temperatures using biochemical, biophysical and crystallographic methods. The crystal structure of xylanase 10B from hyperthermophilic bacterium Thermotoga petrophila RKU-1 (TpXyl10B) has been solved in the native state and in complex with xylobiose. The complex crystal structure showed a classical binding mode shared among other xylanases, which encompasses the -1 and -2 subsites. Interestingly, TpXyl10B displayed a temperature-dependent action mode producing xylobiose and xylotriose at 20°C, and exclusively xylobiose at 90°C as assessed by capillary zone electrophoresis. Moreover, circular dichroism spectroscopy suggested a coupling effect of temperature-induced structural changes with this particular enzymatic behavior. Molecular dynamics simulations supported the CD analysis suggesting that an open conformational state adopted by the catalytic loop (Trp297-Lys326) provokes significant modifications in the product release area (+1,+2 and +3 subsites), which drives the enzymatic activity to the specific release of xylobiose at high temperatures.

PubMed: 21070746
DOI: 10.1016/j.bbrc.2010.11.010

実験手法

X-RAY DIFFRACTION (1.88 Å)