PDBsum entry 2vn4

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protein ligands links
Hydrolase PDB id
Protein chain
599 a.a. *
MAN ×8
BTB ×2
Waters ×361
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Glycoside hydrolase family 15 glucoamylase from hypocrea jecorina
Structure: Glucoamylase. Chain: a. Ec:
Source: Hypocrea jecorina. Organism_taxid: 51453
1.85Å     R-factor:   0.155     R-free:   0.182
Authors: R.Bott,M.Sandgren,H.Hansson
Key ref: R.Bott et al. (2008). Three-dimensional structure of an intact glycoside hydrolase family 15 glucoamylase from Hypocrea jecorina. Biochemistry, 47, 5746-5754. PubMed id: 18457422 DOI: 10.1021/bi702413k
30-Jan-08     Release date:   20-May-08    
Go to PROCHECK summary

Protein chain
No UniProt id for this chain
Struc: 599 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glucan 1,4-alpha-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     polysaccharide metabolic process   2 terms 
  Biochemical function     catalytic activity     5 terms  


DOI no: 10.1021/bi702413k Biochemistry 47:5746-5754 (2008)
PubMed id: 18457422  
Three-dimensional structure of an intact glycoside hydrolase family 15 glucoamylase from Hypocrea jecorina.
R.Bott, M.Saldajeno, W.Cuevas, D.Ward, M.Scheffers, W.Aehle, S.Karkehabadi, M.Sandgren, H.Hansson.
The three-dimensional structure of a complete Hypocrea jecorina glucoamylase has been determined at 1.8 A resolution. The presented structure model includes the catalytic and starch binding domains and traces the course of the 37-residue linker segment. While the structures of other fungal and yeast glucoamylase catalytic and starch binding domains have been determined separately, this is the first intact structure that allows visualization of the juxtaposition of the starch binding domain relative to the catalytic domain. The detailed interactions we see between the catalytic and starch binding domains are confirmed in a second independent structure determination of the enzyme in a second crystal form. This second structure model exhibits an identical conformation compared to the first structure model, which suggests that the H. jecorina glucoamylase structure we report is independent of crystal lattice contact restraints and represents the three-dimensional structure found in solution. The proposed starch binding regions for the starch binding domain are aligned with the catalytic domain in the three-dimensional structure in a manner that supports the hypothesis that the starch binding domain serves to target the glucoamylase at sites where the starch granular matrix is disrupted and where the enzyme might most effectively function.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21152915 J.Marín-Navarro, and J.Polaina (2011).
Glucoamylases: structural and biotechnological aspects.
  Appl Microbiol Biotechnol, 89, 1267-1273.  
20238168 S.Yang, N.Jia, M.Li, and J.Wang (2011).
Heterologous expression and efficient ethanol production of a Rhizopus glucoamylase gene in Saccharomyces cerevisiae.
  Mol Biol Rep, 38, 59-64.  
19682075 C.Christiansen, M.Abou Hachem, S.Janecek, A.Viksø-Nielsen, A.Blennow, and B.Svensson (2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
  FEBS J, 276, 5006-5029.  
19757138 T.M.da Silva, M.Michelin, A.R.Damásio, A.Maller, F.B.Almeida, R.Ruller, R.J.Ward, J.C.Rosa, J.A.Jorge, H.F.Terenzi, and M.d.e. .L.Polizeli (2009).
Purification and biochemical characterization of a novel alpha-glucosidase from Aspergillus niveus.
  Antonie Van Leeuwenhoek, 96, 569-578.  
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