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protein metals links
Hydrolase PDB id
1gcy
Jmol
Contents
Protein chain
415 a.a. *
Metals
_CA ×2
Waters ×222
* Residue conservation analysis
PDB id:
1gcy
Name: Hydrolase
Title: High resolution crystal structure of maltotetraose-forming exo-amylase
Structure: Glucan 1,4-alpha-maltotetrahydrolase. Chain: a. Engineered: yes
Source: Pseudomonas stutzeri. Organism_taxid: 316. Strain: mo-19. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.60Å     R-factor:   0.259     R-free:   0.304
Authors: Y.Mezaki,Y.Katsuya,M.Kubota,Y.Matsuura
Key ref: Y.Mezaki et al. (2001). Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri. Biosci Biotechnol Biochem, 65, 222-225. PubMed id: 11272837 DOI: 10.1271/bbb.65.222
Date:
14-Aug-00     Release date:   30-Aug-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13507  (AMT4_PSEST) -  Glucan 1,4-alpha-maltotetraohydrolase
Seq:
Struc: 		 
Seq:
Struc: 		548 a.a.
415 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.3.2.1.60  - Glucan 1,4-alpha-maltotetraohydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides so as to remove successive maltotetraose residues from the non-reducing chain ends.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
DOI no: 10.1271/bbb.65.222 Biosci Biotechnol Biochem 65:222-225 (2001)
PubMed id: 11272837  
 
 
Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Y.Mezaki, Y.Katsuya, M.Kubota, Y.Matsuura.
 
  ABSTRACT  
 
The intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri (G4-1), which has a raw starch binding domain, has been crystallized. The structure was identified (PDB entry 1GCY) by the molecular replacement method using the structure of its catalytic domain (G4-2). The result showed that the raw starch binding domain is in a disordered state, the corresponding electron densities being almost invisible. Superposition of these two enzyme forms showed evidence for the possible location of the raw starch binding domain (SBD). This crystal is a novel case, in that it forms a regular lattice incorporating flexibly bound SBD in the channel of crystal packing of the catalytic domains.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
18186486 J.Arunachalam, and N.Gautham (2008).
Hydrophobic clusters in protein structures.
  Proteins, 71, 2012-2025.  
12581203 S.Janecek, B.Svensson, and E.A.MacGregor (2003).
Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
  Eur J Biochem, 270, 635-645.  
  12906828 X.Robert, R.Haser, T.E.Gottschalk, F.Ratajczak, H.Driguez, B.Svensson, and N.Aghajari (2003).
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs.
  Structure, 11, 973-984.
PDB codes: 1ht6 1p6w
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 codes are shown on the right.