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PDBsum entry 1fhl

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protein links
Hydrolase PDB id
1fhl
Jmol
Contents
Protein chain
334 a.a. *
Waters ×59
* Residue conservation analysis
PDB id:
1fhl
Name: Hydrolase
Title: Crystal structure of beta-1,4-galactanase from aspergillus aculeatus at 293k
Structure: Beta-1,4-galactanase. Chain: a. Ec: 3.2.1.89
Source: Aspergillus aculeatus. Organism_taxid: 5053
Resolution:
2.30Å     R-factor:   0.166     R-free:   0.245
Authors: C.Ryttersgaard,S.Larsen
Key ref:
C.Ryttersgaard et al. (2002). Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A. Biochemistry, 41, 15135-15143. PubMed id: 12484750 DOI: 10.1021/bi026238c
Date:
02-Aug-00     Release date:   03-Jun-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P48842  (GANA_ASPAC) -  Arabinogalactan endo-beta-1,4-galactanase
Seq:
Struc:
350 a.a.
334 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.89  - Arabinogalactan endo-beta-1,4-galactanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-galactosidic linkages in arabinogalactans.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
DOI no: 10.1021/bi026238c Biochemistry 41:15135-15143 (2002)
PubMed id: 12484750  
 
 
Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A.
C.Ryttersgaard, L.Lo Leggio, P.M.Coutinho, B.Henrissat, S.Larsen.
 
  ABSTRACT  
 
The three-dimensional structure of Aspergillus aculeatus beta-1,4-galactanase (AAGAL), an enzyme involved in pectin degradation, has been determined by multiple isomorphous replacement to 2.3 and 1.8 A resolution at 293 and 100 K, respectively. It represents the first known structure for a polysaccharidase with this specificity and for a member of glycoside hydrolase family 53 (GH-53). The enzyme folds into a (beta/alpha)(8) barrel with the active site cleft located at the C-terminal side of the barrel consistent with the classification of GH-53 in clan GH-A, a superfamily of enzymes with common fold and catalytic machinery but diverse specificities. Putative substrate-enzyme interactions were elucidated by modeling of beta-1,4-linked galactobioses into the possible substrate binding subsites. The structure and modeling studies identified five potential subsites for the binding of galactans, of which one is a pocket suited for accommodating the arabinan side chain in arabinogalactan, one of the natural substrates. A comparison with the substrate binding grooves of other Clan GH-A enzymes suggests that shape complementarity is crucial in determining the specificity of polysaccharidases.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21103910 K.M.Turner, G.Pasut, F.M.Veronese, A.Boyce, and G.Walsh (2011).
Stabilization of a supplemental digestive enzyme by post-translational engineering using chemically-activated polyethylene glycol.
  Biotechnol Lett, 33, 617-621.  
18755688 Y.Zhang, J.Ju, H.Peng, F.Gao, C.Zhou, Y.Zeng, Y.Xue, Y.Li, B.Henrissat, G.F.Gao, and Y.Ma (2008).
Biochemical and Structural Characterization of the Intracellular Mannanase AaManA of Alicyclobacillus acidocaldarius Reveals a Novel Glycoside Hydrolase Family Belonging to Clan GH-A.
  J Biol Chem, 283, 31551-31558.
PDB code: 3civ
17905739 Y.Kitago, S.Karita, N.Watanabe, M.Kamiya, T.Aizawa, K.Sakka, and I.Tanaka (2007).
Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum.
  J Biol Chem, 282, 35703-35711.
PDB codes: 2e0p 2e4t 2eex 2ej1 2eo7 2eqd
17056685 S.Shipkowski, and J.E.Brenchley (2006).
Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases.
  Appl Environ Microbiol, 72, 7730-7738.  
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
16151143 S.W.Hinz, M.I.Pastink, L.A.van den Broek, J.P.Vincken, and A.G.Voragen (2005).
Bifidobacterium longum endogalactanase liberates galactotriose from type I galactans.
  Appl Environ Microbiol, 71, 5501-5510.  
15652973 T.Collins, C.Gerday, and G.Feller (2005).
Xylanases, xylanase families and extremophilic xylanases.
  FEMS Microbiol Rev, 29, 3.  
15308675 M.Kurogochi, S.Nishimura, and Y.C.Lee (2004).
Mechanism-based fluorescent labeling of beta-galactosidases. An efficient method in proteomics for glycoside hydrolases.
  J Biol Chem, 279, 44704-44712.  
12761390 J.Le Nours, C.Ryttersgaard, L.Lo Leggio, P.R.Østergaard, T.V.Borchert, L.L.Christensen, and S.Larsen (2003).
Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.
  Protein Sci, 12, 1195-1204.
PDB codes: 1hjq 1hjs 1hju
14517232 K.Hövel, D.Shallom, K.Niefind, V.Belakhov, G.Shoham, T.Baasov, Y.Shoham, and D.Schomburg (2003).
Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase.
  EMBO J, 22, 4922-4932.
PDB codes: 1pz2 1pz3 1qw8 1qw9
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.