PDBsum entry 1qox

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protein Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
(+ 10 more) 449 a.a. *
Waters ×2448
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Beta-glucosidase from bacillus circulans sp. Alkalophilus
Structure: Beta-glucosidase. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p. Ec:
Source: Bacillus circulans. Organism_taxid: 44160. Strain: alkalophilus
Biol. unit: Homo-Octamer (from PDB file)
2.7Å     R-factor:   0.255    
Authors: N.Hakulinen,J.Rouvinen
Key ref: N.Hakulinen et al. (2000). The crystal structure of beta-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies. J Struct Biol, 129, 69-79. PubMed id: 10675298 DOI: 10.1006/jsbi.1999.4206
24-Nov-99     Release date:   27-Feb-00    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q03506  (BGLA_BACCI) -  Beta-glucosidase
450 a.a.
449 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 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: 10.1006/jsbi.1999.4206 J Struct Biol 129:69-79 (2000)
PubMed id: 10675298  
The crystal structure of beta-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies.
N.Hakulinen, S.Paavilainen, T.Korpela, J.Rouvinen.
Family 1 of glycosyl hydrolases is a large and biologically important group of enzymes. A new three-dimensional structure of this family, beta-glucosidase from Bacillus circulans sp. alkalophilus is reported here. This is the first structure of beta-glucosidase from an alkaliphilic organism. The model was determined by the molecular replacement method and refined to a resolution of 2.7 A. The quaternary structure of B. circulans sp. alkalophilus beta-glucosidase is an octamer and subunits of the octamer show a similar (beta/alpha)(8) barrel fold to that previously reported for other family 1 enzymes. The crystal structure suggested that Cys169 in the active site is substituted. The Cys169 is located near the putative acid/base catalyst Glu166 and it may contribute to the high pH optimum of the enzyme. The crystal structure also revealed that the asymmetric unit contains two octamers which have a clear binding interaction with each other. The ability of the octamers to link with each other suggested that beta-glucosidase from Bacillus circulans sp. alkalophilus is able to form long polymeric assemblies, at least in the crystalline state.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21046402 H.Xu, A.S.Xiong, W.Zhao, Y.S.Tian, R.H.Peng, J.M.Chen, and Q.H.Yao (2011).
Characterization of a Glucose-, Xylose-, Sucrose-, and D: -Galactose-Stimulated β-Glucosidase from the Alkalophilic Bacterium Bacillus halodurans C-125.
  Curr Microbiol, 62, 833-839.  
20376631 C.S.Park, M.H.Yoo, K.H.Noh, and D.K.Oh (2010).
Biotransformation of ginsenosides by hydrolyzing the sugar moieties of ginsenosides using microbial glycosidases.
  Appl Microbiol Biotechnol, 87, 9.  
19214809 A.O.Lima, D.F.Davis, G.Swiatek, J.K.McCarthy, D.Yernool, A.A.Pizzirani-Kleiner, and D.E.Eveleigh (2009).
Evaluation of GFP Tag as a Screening Reporter in Directed Evolution of a Hyperthermophilic beta-Glucosidase.
  Mol Biotechnol, 42, 205-215.  
17503162 M.León, P.Isorna, M.Menéndez, J.Sanz-Aparicio, and J.Polaina (2007).
Comparative study and mutational analysis of distinctive structural elements of hyperthermophilic enzymes.
  Protein J, 26, 435-444.
PDB code: 1uwi
17009294 K.Krause, and E.Kothe (2006).
Use of RNA fingerprinting to identify fungal genes specifically expressed during ectomycorrhizal interaction.
  J Basic Microbiol, 46, 387-399.  
15252054 Y.W.Kim, S.S.Lee, R.A.Warren, and S.G.Withers (2004).
Directed evolution of a glycosynthase from Agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire.
  J Biol Chem, 279, 42787-42793.  
12596260 E.Bismuto, F.Febbraio, S.Limongelli, R.Briante, and R.Nucci (2003).
Dynamic fluorescence studies of beta-glycosidase mutants from Sulfolobus solfataricus: effects of single mutations on protein thermostability.
  Proteins, 51, 10-20.  
12012341 B.Cobucci-Ponzano, M.Moracci, B.Di Lauro, M.Ciaramella, R.D'Avino, and M.Rossi (2002).
Ionic network at the C-terminus of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization.
  Proteins, 48, 98.  
11900558 T.Kaper, H.H.van Heusden, B.van Loo, A.Vasella, J.van der Oost, and Vos (2002).
Substrate specificity engineering of beta-mannosidase and beta-glucosidase from Pyrococcus by exchange of unique active site residues.
  Biochemistry, 41, 4147-4155.  
12487426 Y.Bhatia, S.Mishra, and V.S.Bisaria (2002).
Microbial beta-glucosidases: cloning, properties, and applications.
  Crit Rev Biotechnol, 22, 375-407.  
11374467 H.Zhang, and S.H.Neau (2001).
In vitro degradation of chitosan by a commercial enzyme preparation: effect of molecular weight and degree of deacetylation.
  Biomaterials, 22, 1653-1658.  
11134937 J.Vévodová, J.Marek, J.Zouhar, B.Brzobohatý, and X.D.Su (2001).
Purification, crystallization and preliminary X-ray analysis of a maize cytokinin glucoside specific beta-glucosidase.
  Acta Crystallogr D Biol Crystallogr, 57, 140-142.  
11679733 X.Y.He, X.Q.Wang, S.J.Yang, W.R.Chang, and D.C.Liang (2001).
Overexpression, purification, crystallization and preliminary crystallographic studies on a thermostable beta-glycosidase from Thermus nonproteolyticus HG102.
  Acta Crystallogr D Biol Crystallogr, 57, 1650-1651.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.