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PDBsum entry 4iih

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
4iih
Jmol
Contents
Protein chains
833 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN-MAN
×5
NAG ×5
NAG-NAG-BMA ×4
NAG-NAG
NAG-NAG-BMA-MAN-
MAN-MAN-MAN-MAN-
MAN-MAN
×2
MRD ×4
TCB ×2
NAG-NAG-BMA-MAN-
MAN-MAN
NAG-NAG-BMA-MAN-
MAN-MAN-MAN-MAN
Waters ×1607
PDB id:
4iih
Name: Hydrolase
Title: Crystal structure of beta-glucosidase 1 from aspergillus acu complex with thiocellobiose
Structure: Beta-glucosidase 1. Chain: a, b. Synonym: beta-d-glucoside glucohydrolase, cellobiase, genti engineered: yes
Source: Aspergillus aculeatus. Organism_taxid: 5053. Strain: f-50. Gene: bgl1. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062.
Resolution:
2.00Å     R-factor:   0.142     R-free:   0.181
Authors: K.Suzuki,J.Sumitani,T.Kawaguchi,S.Fushinobu
Key ref: K.Suzuki et al. (2013). Crystal structures of glycoside hydrolase family 3 β-glucosidase 1 from Aspergillus aculeatus. Biochem J, 452, 211-221. PubMed id: 23537284 DOI: 10.1042/BJ20130054
Date:
20-Dec-12     Release date:   10-Apr-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P48825  (BGL1_ASPAC) -  Beta-glucosidase 1
Seq:
Struc:
 
Seq:
Struc:
860 a.a.
833 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.21  - Beta-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
DOI no: 10.1042/BJ20130054 Biochem J 452:211-221 (2013)
PubMed id: 23537284  
 
 
Crystal structures of glycoside hydrolase family 3 β-glucosidase 1 from Aspergillus aculeatus.
K.Suzuki, J.Sumitani, Y.W.Nam, T.Nishimaki, S.Tani, T.Wakagi, T.Kawaguchi, S.Fushinobu.
 
  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.