4IIH
Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose
Summary for 4IIH
| Entry DOI | 10.2210/pdb4iih/pdb |
| Related | 4IIB 4IIC 4IID 4IIE 4IIF 4IIG |
| Related PRD ID | PRD_900034 |
| Descriptor | Beta-glucosidase 1, beta-D-glucopyranose-(1-4)-4-thio-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total) |
| Functional Keywords | tim barrel, hydrolase, high-mannose n-glycosylations, extracellular |
| Biological source | Aspergillus aculeatus |
| Total number of polymer chains | 2 |
| Total formula weight | 199617.07 |
| Authors | Suzuki, K.,Sumitani, J.,Kawaguchi, T.,Fushinobu, S. (deposition date: 2012-12-20, release date: 2013-04-10, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 23537284DOI: 10.1042/BJ20130054 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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