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PDBsum entry 4hhp

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
4hhp
Jmol PyMol
Contents
Protein chains
249 a.a.
Ligands
GOL ×2
SO4
Waters ×429
PDB id:
4hhp
Name: Isomerase
Title: Crystal structure of triosephosphate isomerase from trypanos mutant e105d
Structure: Triosephosphate isomerase, glycosomal. Chain: a, b. Synonym: tim, triose-phosphate isomerase. Engineered: yes. Mutation: yes
Source: Trypanosoma cruzi. Organism_taxid: 5693. Strain: mexican ninoa. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.50Å     R-factor:   0.167     R-free:   0.196
Authors: A.Hernandez-Santoyo,Y.Aguirre-Fuentes,A.Torres-Larios,A.Gome M.T.De Gomez-Puyou
Key ref: Y.Aguirre et al. (2014). Different contribution of conserved amino acids to the global properties of triosephosphate isomerases. Proteins, 82, 323-335. PubMed id: 23966267 DOI: 10.1002/prot.24398
Date:
10-Oct-12     Release date:   16-Oct-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P52270  (TPIS_TRYCR) -  Triosephosphate isomerase, glycosomal
Seq:
Struc:
251 a.a.
249 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 = GOL)
matches with 60.00% similarity
= glycerone phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     glycosome   2 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1002/prot.24398 Proteins 82:323-335 (2014)
PubMed id: 23966267  
 
 
Different contribution of conserved amino acids to the global properties of triosephosphate isomerases.
Y.Aguirre, N.Cabrera, B.Aguirre, R.Pérez-Montfort, A.Hernandez-Santoyo, H.Reyes-Vivas, S.Enríquez-Flores, M.T.de Gómez-Puyou, A.Gómez-Puyou, J.M.Sanchez-Ruiz, M.Costas.
 
  ABSTRACT  
 
It is generally assumed that the amino acids that exist in all homologous enzymes correspond to residues that participate in catalysis, or that are essential for folding and stability. Although this holds for catalytic residues, the function of conserved noncatalytic residues is not clear. It is not known if such residues are of equal importance and have the same role in different homologous enzymes. In humans, the E104D mutation in triosephosphate isomerase (TIM) is the most frequent mutation in the autosomal diseases named "TPI deficiencies." We explored if the E104D mutation has the same impact in TIMs from four different organisms (Homo sapiens, Giardia lamblia, Trypanosoma cruzi, and T. brucei). The catalytic properties were not significantly affected by the mutation, but it affected the rate and extent of formation of active dimers from unfolded monomers differently. Scanning calorimetry experiments indicated that the mutation was in all cases destabilizing, but the mutation effect on rates of irreversible denaturation and transition-state energetics were drastically dependent on the TIM background. For instance, the E104D mutation produce changes in activation energy ranging from 430 kJ mol(-1) in HsTIM to -78 kJ mol(-1) in TcTIM. Thus, in TIM the role of a conserved noncatalytic residue is drastically dependent on its molecular background. Accordingly, it would seem that because each protein has a particular sequence, and a distinctive set of amino acid interactions, it should be regarded as a unique entity that has evolved for function and stability in the organisms to which it belongs. Proteins 2014; 82:323-335. © 2013 Wiley Periodicals, Inc.
 

 

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