4IIC

Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine

4IIC の概要

• エントリーDOI: 10.2210/pdb4iic/pdb
• 関連するPDBエントリー: 4IIB 4IID 4IIE 4IIF 4IIG 4IIH
• 分子名称: Beta-glucosidase 1, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (16 entities in total)
• 機能のキーワード: tim barrel, hydrolase, high-mannose n-glycosylations, extracellular
• 由来する生物種: Aspergillus aculeatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 198828.45

構造登録者

Suzuki, K.,Sumitani, J.,Kawaguchi, T.,Fushinobu, S. (登録日: 2012-12-20, 公開日: 2013-04-10, 最終更新日: 2024-10-30)

主引用文献

Suzuki, K.,Sumitani, J.,Nam, Y.W.,Nishimaki, T.,Tani, S.,Wakagi, T.,Kawaguchi, T.,Fushinobu, S.
Crystal structures of glycoside hydrolase family 3 beta-glucosidase 1 from Aspergillus aculeatus
Biochem.J., 452:211-221, 2013

PubMed Abstract: GH3 (glycoside hydrolase family 3) BGLs (β-glucosidases) from filamentous fungi have been widely and commercially used for the supplementation of cellulases. AaBGL1 (Aspergillus aculeatus BGL1) belongs to the GH3 and shows high activity towards cellooligosaccharides up to high degree of polymerization. In the present study we determined the crystal structure of AaBGL1. In addition to the substrate-free structure, the structures of complexes with glucose and various inhibitors were determined. The structure of AaBGL1 is highly glycosylated with 88 monosaccharides (18 N-glycan chains) in the dimer. The largest N-glycan chain comprises ten monosaccharides and is one of the largest glycans ever observed in protein crystal structures. A prominent insertion region exists in a fibronectin type III domain, and this region extends to cover a wide surface area of the enzyme. The subsite +1 of AaBGL1 is highly hydrophobic. Three aromatic residues are present at subsite +1 and are located in short loop regions that are uniquely present in this enzyme. There is a long cleft extending from subsite +1, which appears to be suitable for binding long cellooligosaccharides. The crystal structures of AaBGL1 from the present study provide an important structural basis for the technical improvement of enzymatic cellulosic biomass conversion.

PubMed: 23537284
DOI: 10.1042/BJ20130054

実験手法

X-RAY DIFFRACTION (1.9 Å)