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PDBsum entry 2vn4
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Hydrolase PDB id
2vn4

 

 

 

 

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Contents
Protein chain
599 a.a. *
Ligands
NAG-NAG
MAN ×8
NAG
BTB ×2
Waters ×361
* Residue conservation analysis
PDB id:
2vn4
Name: Hydrolase
Title: Glycoside hydrolase family 15 glucoamylase from hypocrea jecorina
Structure: Glucoamylase. Chain: a. Ec: 3.2.1.3
Source: Hypocrea jecorina. Organism_taxid: 51453
Resolution:
1.85Å     R-factor:   0.156     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
Date:
30-Jan-08     Release date:   20-May-08    
PROCHECK
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 Headers
 References

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

 

 
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.
 
  ABSTRACT  
 
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.  
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.

 

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