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PDBsum entry 1aq0

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
1aq0
Jmol
Contents
Protein chains
306 a.a. *
Ligands
NAG-NAG ×2
ACT ×2
Waters ×418
* Residue conservation analysis
PDB id:
1aq0
Name: Hydrolase
Title: Barley 1,3-1,4-beta-glucanase in monoclinic space group
Structure: 1,3-1,4-beta-glucanase. Chain: a, b. Synonym: 1,3-1,4-beta-d-glucan 4-glucanohydrolase. Other_details: isoenzyme 2
Source: Hordeum vulgare. Organism_taxid: 4513
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.170     R-free:   0.213
Authors: J.J.Mueller,K.K.Thomsen,U.Heinemann
Key ref:
J.J.Müller et al. (1998). Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase. J Biol Chem, 273, 3438-3446. PubMed id: 9452466 DOI: 10.1074/jbc.273.6.3438
Date:
05-Aug-97     Release date:   11-Feb-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P12257  (GUB2_HORVU) -  Lichenase-2 (Fragment)
Seq:
Struc:
312 a.a.
306 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.73  - Licheninase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,4-beta-D-glycosidic linkages in beta-D-glucans containing 1,3- and 1,4-bonds.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
DOI no: 10.1074/jbc.273.6.3438 J Biol Chem 273:3438-3446 (1998)
PubMed id: 9452466  
 
 
Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase.
J.J.Müller, K.K.Thomsen, U.Heinemann.
 
  ABSTRACT  
 
Both plants and bacteria produce enzymes capable of degrading the mixed-linked beta-glucan of the endosperm cell walls of cereal grains. The enzymes share the specificity for beta-1,4 glycosyl bonds of O-3-substituted glucose units in linear polysaccharides and a similar cleavage mechanism but are unrelated in sequence and tertiary structure. The three-dimensional structure of the 1,3-1, 4-beta-glucanase isoenzyme EII from barley was determined from monoclinic crystals at a resolution of 2.0 A. The protein is folded into a betaalpha8 barrel structure as has been shown previously (Varghese, J. N., Garrett, T. P. J., Colman, P. M., Chen, L., Hoj, P. B., and Fincher, G. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2785-2789) by diffraction analysis at lower resolution of tetragonal crystals. It contains one N-glycosylation site which is described in detail with the sugar moieties attached to residue Asn190. The geometry and hydration of the barley 1,3-1,4-beta-glucanase is analyzed; a model beta-glucan fragment is placed into the binding site by molecular dynamics simulation, and the beta-glucan binding grooves of the plant and bacterial enzymes are compared. Their active sites are shown to have a small number of common features in generally dissimilar geometries that serve to explain both the identical substrate specificity and the observed differences in inhibitor binding.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Stereographic cartoon of the molecular structure of the barley 1,3-1,4- -glucanase, isoenzyme EII. The view is through the active site channel of the enzyme. Arrows indicate -strands, and wound ribbons indicate -helices. No arrow is drawn for -strand^ number 8 consisting of only two residues. The two catalytic glutamic^ acid residues 232 and 288 of EII are drawn in ball-and-stick representation, as well as the carbohydrate attached to residue Asn190. Drawn with MOLSCRIPT (39).
Figure 5.
Fig. 5. Stereographic drawings of the substrate binding cleft of barley 1,3-1,4- -glucanase and of the hybrid Bacillus 1,3-1,4- -glucanase^ H(A16-M). Top, barley 1,3-1,4- -glucanase, active site atoms of Glu232, Tyr33, and Glu288 are labeled. Bottom, H(A16-M). The active site residues Glu105, Tyr94, and Glu109 are labeled. Water molecules binding to the corresponding cleft are shown as blue spheres. The maps defining the clefts were estimated^ by SURFNET (32). Drawn with BOBSCRIPT (42) and RASTER3D (43).
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (1998, 273, 3438-3446) copyright 1998.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20043351 Q.Guo, W.Zhang, L.L.Ma, Q.H.Chen, J.C.Chen, H.B.Zhang, H.Ruan, and G.Q.He (2010).
A food-grade industrial arming yeast expressing beta-1,3-1,4-glucanase with enhanced thermal stability.
  J Zhejiang Univ Sci B, 11, 41-51.  
19018102 L.C.Tsai, H.C.Huang, C.H.Hsiao, Y.N.Chiang, L.F.Shyur, Y.S.Lin, and S.H.Lee (2008).
Mutational and structural studies of the active-site residues in truncated Fibrobacter succinogenes1,3-1,4-beta-D-glucanase.
  Acta Crystallogr D Biol Crystallogr, 64, 1259-1266.  
18663584 L.C.Tsai, Y.N.Chen, and L.F.Shyur (2008).
Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-D-glucanases.
  J Comput Aided Mol Des, 22, 915-923.  
  18678950 S.Yang, Y.Wang, Z.Jiang, and C.Hua (2008).
Crystallization and preliminary X-ray analysis of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 754-756.  
16421930 V.Receveur-Bréchot, M.Czjzek, A.Barre, A.Roussel, W.J.Peumans, E.J.Van Damme, and P.Rougé (2006).
Crystal structure at 1.45-A resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome.
  Proteins, 63, 235-242.
PDB code: 2cyg
15545660 J.G.Bishop, D.R.Ripoll, S.Bashir, C.M.Damasceno, J.D.Seeds, and J.K.Rose (2005).
Selection on Glycine beta-1,3-endoglucanase genes differentially inhibited by a Phytophthora glucanase inhibitor protein.
  Genetics, 169, 1009-1019.  
  16508094 Z.Pang, Y.N.Kang, M.Ban, M.Oda, R.Kobayashi, M.Ohnishi, and B.Mikami (2005).
Crystallization and preliminary crystallographic analysis of endo-1,3-beta-glucanase from Arthrobacter sp.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 68-70.  
11526326 L.C.Tsai, L.F.Shyur, S.S.Lin, and H.S.Yuan (2001).
Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes.
  Acta Crystallogr D Biol Crystallogr, 57, 1303-1306.  
10672030 W.J.Peumans, A.Barre, V.Derycke, P.Rougé, W.Zhang, G.D.May, J.A.Delcour, F.Van Leuven, and E.J.Van Damme (2000).
Purification, characterization and structural analysis of an abundant beta-1,3-glucanase from banana fruit.
  Eur J Biochem, 267, 1188-1195.  
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.