3AMC

Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au

3AMC の概要

• エントリーDOI: 10.2210/pdb3amc/pdb
• 関連するPDBエントリー: 3AMD 3AMG 3AOF 3AZR 3AZS 3AZT
• 分子名称: Endoglucanase (2 entities in total)
• 機能のキーワード: glycosyl hydrolase family 5, cellulase, biofuel, hyperthermostable, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74877.05

構造登録者

Wu, T.H.,Huang, C.H.,Ko, T.P.,Lai, H.L.,Ma, Y.,Cheng, Y.S.,Liu, J.R.,Guo, R.T. (登録日: 2010-08-19, 公開日: 2011-08-10, 最終更新日: 2024-03-13)

主引用文献

Wu, T.H.,Huang, C.H.,Ko, T.P.,Lai, H.L.,Ma, Y.,Chen, C.C.,Cheng, Y.S.,Liu, J.R.,Guo, R.T.
Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose
Biochim.Biophys.Acta, 1814:1832-1840, 2011

PubMed Abstract: The hyperthermophilic endoglucanase Cel5A from Thermotoga maritima can find applications in lignocellulosic biofuel production, because it catalyzes the hydrolysis of glucan- and mannan-based polysaccharides. Here, we report the crystal structures in apo-form and in complex with three ligands, cellotetraose, cellobiose and mannotriose, at 1.29Å to 2.40Å resolution. The open carbohydrate-binding cavity which can accommodate oligosaccharide substrates with extensively branched chains explained the dual specificity of the enzyme. Combining our structural information and the previous kinetic data, it is suggested that this enzyme prefers β-glucosyl and β-mannosyl moieties at the reducing end and uses two conserved catalytic residues, E253 (nucleophile) and E136 (general acid/base), to hydrolyze the glycosidic bonds. Moreover, our results also suggest that the wide spectrum of Tm_Cel5A substrates might be due to the lack of steric hindrance around the C2-hydroxyl group of the glucose or mannose unit from active-site residues.

PubMed: 21839861
DOI: 10.1016/j.bbapap.2011.07.020

実験手法

X-RAY DIFFRACTION (1.4 Å)