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PDBsum entry 4ff7

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4ff7
Jmol
Contents
Protein chains
247 a.a.
Ligands
PGA
GOL ×12
SO4 ×2
PO4 ×3
Metals
_NA
Waters ×318
PDB id:
4ff7
Name: Oxidoreductase
Title: Structure of c126s mutant of saccharomyces cerevisiae triose isomerase
Structure: Triosephosphate isomerase. Chain: a, b. Synonym: tim, triose-phosphate isomerase. Engineered: yes. Mutation: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: tpi1, ydr050c, yd9609.05c. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.86Å     R-factor:   0.177     R-free:   0.212
Authors: A.Rodriguez-Romero,A.Hernandez-Santoyo
Key ref: A.Hernández-Santoyo et al. (2012). Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability. Int J Mol Sci, 13, 10010-10021. PubMed id: 22949845
Date:
31-May-12     Release date:   22-Aug-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00942  (TPIS_YEAST) -  Triosephosphate isomerase
Seq:
Struc:
248 a.a.
247 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.5.3.1.1  - Triose-phosphate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-glyceraldehyde 3-phosphate = glycerone phosphate
D-glyceraldehyde 3-phosphate
Bound ligand (Het Group name = PGA)
matches with 72.73% similarity
= glycerone phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   1 term 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
Int J Mol Sci 13:10010-10021 (2012)
PubMed id: 22949845  
 
 
Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.
A.Hernández-Santoyo, L.Domínguez-Ramírez, C.A.Reyes-López, E.González-Mondragón, A.Hernández-Arana, A.Rodríguez-Romero.
 
  ABSTRACT  
 
All the members of the triosephosphate isomerase (TIM) family possess a cystein residue (Cys126) located near the catalytically essential Glu165. The evolutionarily conserved Cys126, however, does not seem to play a significant role in the catalytic activity. On the other hand, substitution of this residue by other amino acid residues destabilizes the dimeric enzyme, especially when Cys is replaced by Ser. In trying to assess the origin of this destabilization we have determined the crystal structure of Saccharomyces cerevisiae TIM (ScTIM) at 1.86 Å resolution in the presence of PGA, which is only bound to one subunit. Comparisons of the wild type and mutant structures reveal that a change in the orientation of the Ser hydroxyl group, with respect to the Cys sulfhydryl group, leads to penetration of water molecules and apparent destabilization of residues 132-138. The latter results were confirmed by means of Molecular Dynamics, which showed that this region, in the mutated enzyme, collapses at about 70 ns.