PDBsum entry 2ayh

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protein metals links
Hydrolase (glucanase) PDB id
Protein chain
214 a.a. *
Waters ×202
* Residue conservation analysis
PDB id:
Name: Hydrolase (glucanase)
Title: Crystal and molecular structure at 1.6 angstroms resolution of the hybrid bacillus endo-1,3-1,4-beta-d-glucan 4- glucanohydrolase h(a16-m)
Structure: 1,3-1,4-beta-d-glucan 4-glucanohydrolase. Chain: a. Engineered: yes
Source: Hybrid. Organism_taxid: 37965. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.60Å     R-factor:   0.143    
Authors: M.Hahn,T.Keitel,U.Heinemann
Key ref: M.Hahn et al. (1995). Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M). Eur J Biochem, 232, 849-858. PubMed id: 7588726
02-Feb-95     Release date:   31-Mar-95    
Supersedes: 1ayh
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P23904  (GUB_PAEMA) -  Beta-glucanase
237 a.a.
214 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 11 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - 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  


Eur J Biochem 232:849-858 (1995)
PubMed id: 7588726  
Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M).
M.Hahn, T.Keitel, U.Heinemann.
H(A16-M) is a hybrid endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus. Its crystal structure was refined using synchrotron X-ray diffraction data up to a maximal resolution of 0.16 nm. The R value of the resulting model is 14.3% against 21,032 reflections > 2 sigma. 93% of the amino acid residues are in the most favorable regions of the Ramachandran diagram, and geometrical parameters are in accordance with other proteins solved at high resolution. As shown earlier [Keitel, T., Simon, O., Borriss, R. & Heinemann, U. (1993) Proc. Natl Acad. Sci. USA 90, 5287-5291], the protein folds into a compact jellyroll-type beta-sheet structure. A systematic analysis of the secondary structure reveals the presence of two major antiparallel beta-sheets and a three-stranded minor mixed sheet. Amino acid residues involved in catalysis and substrate binding are located inside a deep channel spanning the surface of the protein. To investigate the stereochemical cause of the observed specificity of endo-1,3-1,4-beta-D-glucan 4-glucanohydrolases towards beta-1,4 glycosyl bonds adjacent to beta-1,3 bonds, the high-resolution crystal structure has been used to model an enzyme-substrate complex. It is proposed that productive substrate binding to the subsites p1, p2 and p3 of H(A16-M) requires a beta-1,3 linkage between glucose units bound to p1 and p2.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19435780 C.E.McGrath, T.V.Vuong, and D.B.Wilson (2009).
Site-directed mutagenesis to probe catalysis by a Thermobifida fusca beta-1,3-glucanase (Lam81A).
  Protein Eng Des Sel, 22, 375-382.  
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.  
17879342 G.Fibriansah, S.Masuda, N.Koizumi, S.Nakamura, and T.Kumasaka (2007).
The 1.3 A crystal structure of a novel endo-beta-1,3-glucanase of glycoside hydrolase family 16 from alkaliphilic Nocardiopsis sp. strain F96.
  Proteins, 69, 683-690.
PDB code: 2hyk
17329246 M.Hrmova, V.Farkas, J.Lahnstein, and G.B.Fincher (2007).
A Barley xyloglucan xyloglucosyl transferase covalently links xyloglucan, cellulosic substrates, and (1,3;1,4)-beta-D-glucans.
  J Biol Chem, 282, 12951-12962.  
15557263 M.Strohmeier, M.Hrmova, M.Fischer, A.J.Harvey, G.B.Fincher, and J.Pleiss (2004).
Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae.
  Protein Sci, 13, 3200-3213.  
11435116 G.Michel, L.Chantalat, E.Duee, T.Barbeyron, B.Henrissat, B.Kloareg, and O.Dideberg (2001).
The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.
  Structure, 9, 513-525.
PDB code: 1dyp
11757657 M.Faijes, J.K.Fairweather, H.Driguez, and A.Planas (2001).
Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity: a straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4-beta-glucanases.
  Chemistry, 7, 4651-4655.  
11150614 A.Planas (2000).
Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
  Biochim Biophys Acta, 1543, 361-382.  
10632706 B.O.Petersen, M.Krah, J.O.Duus, and K.K.Thomsen (2000).
A transglycosylating 1,3(4)-beta-glucanase from rhodothermus marinus NMR analysis of enzyme reactions.
  Eur J Biochem, 267, 361-369.  
  10210191 D.H.Juers, R.E.Huber, and B.W.Matthews (1999).
Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases.
  Protein Sci, 8, 122-136.  
10587432 K.Piotukh, V.Serra, R.Borriss, and A.Planas (1999).
Protein-carbohydrate interactions defining substrate specificity in Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases as dissected by mutational analysis.
  Biochemistry, 38, 16092-16104.  
9489923 J.Aÿ, M.Hahn, K.Decanniere, K.Piotukh, R.Borriss, and U.Heinemann (1998).
Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases.
  Proteins, 30, 155-167.
PDB codes: 1ajk 1ajo
9452466 J.J.Müller, K.K.Thomsen, and U.Heinemann (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.
PDB code: 1aq0
9698381 J.L.Viladot, Ramon, O.Durany, and A.Planas (1998).
Probing the mechanism of Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues.
  Biochemistry, 37, 11332-11342.  
9737854 P.E.Johnson, A.L.Creagh, E.Brun, K.Joe, P.Tomme, C.A.Haynes, and L.P.McIntosh (1998).
Calcium binding by the N-terminal cellulose-binding domain from Cellulomonas fimi beta-1,4-glucanase CenC.
  Biochemistry, 37, 12772-12781.  
9148909 J.Pons, E.Querol, and A.Planas (1997).
Mutational analysis of the major loop of Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases. Effects on protein stability and substrate binding.
  J Biol Chem, 272, 13006-13012.  
9153431 L.F.Mackenzie, G.J.Davies, M.Schülein, and S.G.Withers (1997).
Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry.
  Biochemistry, 36, 5893-5901.  
9395451 Y.Gueguen, W.G.Voorhorst, J.van der Oost, and Vos (1997).
Molecular and biochemical characterization of an endo-beta-1,3- glucanase of the hyperthermophilic archaeon Pyrococcus furiosus.
  J Biol Chem, 272, 31258-31264.  
  8931144 K.Welfle, R.Misselwitz, O.Politz, R.Borriss, and H.Welfle (1996).
Individual amino acids in the N-terminal loop region determine the thermostability and unfolding characteristics of bacterial glucanases.
  Protein Sci, 5, 2255-2265.  
8916925 P.E.Johnson, M.D.Joshi, P.Tomme, D.G.Kilburn, and L.P.McIntosh (1996).
Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy.
  Biochemistry, 35, 14381-14394.
PDB codes: 1ulo 1ulp
8905079 R.A.Warren (1996).
Microbial hydrolysis of polysaccharides.
  Annu Rev Microbiol, 50, 183-212.  
9007269 V.Moreau, J.L.Viladot, E.Samain, A.Planas, and H.Driguez (1996).
Design and chemoenzymatic synthesis of thiooligosaccharide inhibitors of 1,3:1,4-beta-D-glucanases.
  Bioorg Med Chem, 4, 1849-1855.  
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.