spacer
spacer

PDBsum entry 1wo2

Go to PDB code: 
protein ligands metals links
Hydrolase PDB id
1wo2
Jmol
Contents
Protein chain
496 a.a. *
Ligands
GLC-GLC-BGC ×2
GLC-BGC
EDO ×6
Metals
_CL
_CA
Waters ×749
* Residue conservation analysis
PDB id:
1wo2
Name: Hydrolase
Title: Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion
Structure: Alpha-amylase, pancreatic. Chain: a. Synonym: 1,4-alpha-d-glucan glucanohydrolase. Ec: 3.2.1.1
Source: Sus scrofa. Pig. Organism_taxid: 9823. Tissue: pancreas
Resolution:
2.01Å     R-factor:   0.159     R-free:   0.184
Authors: M.Qian,F.Payan,V.Nahoum
Key ref:
M.Qian et al. (2005). Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase. Biochemistry, 44, 3194-3201. PubMed id: 15736930 DOI: 10.1021/bi048201t
Date:
11-Aug-04     Release date:   15-Mar-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00690  (AMYP_PIG) -  Pancreatic alpha-amylase
Seq:
Struc:
511 a.a.
496 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.1  - Alpha-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
DOI no: 10.1021/bi048201t Biochemistry 44:3194-3201 (2005)
PubMed id: 15736930  
 
 
Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase.
M.Qian, e.l. .H.Ajandouz, F.Payan, V.Nahoum.
 
  ABSTRACT  
 
Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the alpha-amylase family, is involved in the degradation of starch. Like some other members of this family, PPA requires chloride to reach maximum activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography. A conspicuous reorientation of the acid/base catalyst Glu233 residue was found to occur. The structural results, along with kinetic data, show that the acid/base catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride ions. The present study therefore explains the mechanism of PPA activation by chloride ions.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21529256 N.Ngernyuang, I.Kobayashi, A.Promboon, S.Ratanapo, T.Tamura, and L.Ngernsiri (2011).
Cloning and expression analysis of the Bombyx mori α-amylase gene (Amy) from the indigenous Thai silkworm strain, Nanglai.
  J Insect Sci, 11, 38.  
20222716 S.B.Larson, J.S.Day, and A.McPherson (2010).
X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin.
  Biochemistry, 49, 3101-3115.
PDB codes: 3l2l 3l2m
17729287 J.C.Marx, J.Poncin, J.P.Simorre, P.W.Ramteke, and G.Feller (2008).
The noncatalytic triad of alpha-amylases: a novel structural motif involved in conformational stability.
  Proteins, 70, 320-328.  
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.