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PDBsum entry 1m6j

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protein Protein-protein interface(s) links
Isomerase PDB id
1m6j
Jmol
Contents
Protein chains
260 a.a. *
Waters ×783
* Residue conservation analysis
PDB id:
1m6j
Name: Isomerase
Title: Crystal structure of triosephosphate isomerase from entamoeba histolytica
Structure: Triosephosphate isomerase. Chain: a, b. Synonym: tim, tpi. Engineered: yes
Source: Entamoeba histolytica. Organism_taxid: 5759. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.50Å     R-factor:   0.184     R-free:   0.206
Authors: A.Rodriguez-Romero,A.Hernandez-Santoyo,D.A.Fernandez-Velasco
Key ref:
A.Rodríguez-Romero et al. (2002). Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica. J Mol Biol, 322, 669-675. PubMed id: 12270704 DOI: 10.1016/S0022-2836(02)00809-4
Date:
16-Jul-02     Release date:   12-Oct-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O02611  (TPIS_ENTHI) -  Triosephosphate isomerase
Seq:
Struc:
261 a.a.
260 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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
= glycerone phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/S0022-2836(02)00809-4 J Mol Biol 322:669-675 (2002)
PubMed id: 12270704  
 
 
Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica.
A.Rodríguez-Romero, A.Hernández-Santoyo, L.del Pozo Yauner, A.Kornhauser, D.A.Fernández-Velasco.
 
  ABSTRACT  
 
Triosephosphate isomerase (TIM) has been proposed as a target for drug design. TIMs from several parasites have a cysteine residue at the dimer interface, whose derivatization with thiol-specific reagents induces enzyme inactivation and aggregation. TIMs lacking this residue, such as human TIM, are less affected. TIM from Entamoeba histolytica (EhTIM) has the interface cysteine residue and presents more than ten insertions when compared with the enzyme from other pathogens. To gain further insight into the role that interface residues play in the stability and reactivity of these enzymes, we determined the high-resolution structure and characterized the effect of methylmethane thiosulfonate (MMTS) on the activity and conformational properties of EhTIM. The structure of this enzyme was determined at 1.5A resolution using molecular replacement, observing that the dimer is not symmetric. EhTIM is completely inactivated by MMTS, and dissociated into stable monomers that possess considerable secondary structure. Structural and spectroscopic analysis of EhTIM and comparison with TIMs from other pathogens reveal that conformational rearrangements of the interface after dissociation, as well as intramonomeric contacts formed by the inserted residues, may contribute to the unusual stability of the derivatized EhTIM monomer.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. The 2F[o] -F[c] density maps. Stereo view of the interface Cys14 surrounded by residues of the facing subunit (loop 3). Cys14 SgH (monomer B) and His86 Nd1 (monomer A) are at hydrogen bond distance (top panel). The water network at the surface of the enzyme near Lys129 and Pro96 showing ringed water structure (bottom panel). The maps are contoured at the 1s level.
Figure 3.
Figure 3. Structural comparison of triosephosphate isomerases. (a) C^a superposition of EhTIM (green), TbTIM (blue) and TcTIM (orange). Two insertions of the EhTIM structure are indicated (residues 36-38 and 59-62). (b) C^a superposition of monomers A (green) and B (blue) in EhTIM, differences at loop 3 and 6 are evident. These Figures were created with GRASP.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 322, 669-675) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19261703 S.S.Thakur, P.D.Deepalakshmi, P.Gayathri, M.Banerjee, M.R.Murthy, and P.Balaram (2009).
Detection of the protein dimers, multiple monomeric states and hydrated forms of Plasmodium falciparum triosephosphate isomerase in the gas phase.
  Protein Eng Des Sel, 22, 289-304.  
17280493 A.R.Karala, and L.W.Ruddock (2007).
Does s-methyl methanethiosulfonate trap the thiol-disulfide state of proteins?
  Antioxid Redox Signal, 9, 527-531.  
17989778 V.Olivares-Illana, A.Rodríguez-Romero, I.Becker, M.Berzunza, J.García, R.Pérez-Montfort, N.Cabrera, F.López-Calahorra, M.T.de Gómez-Puyou, and A.Gómez-Puyou (2007).
Perturbation of the Dimer Interface of Triosephosphate Isomerase and its Effect on Trypanosoma cruzi.
  PLoS Negl Trop Dis, 1, e1.
PDB code: 2oma
17221869 V.Zomosa-Signoret, B.Aguirre-López, G.Hernández-Alcántara, R.Pérez-Montfort, M.T.de Gómez-Puyou, and A.Gómez-Puyou (2007).
Crosstalk between the subunits of the homodimeric enzyme triosephosphate isomerase.
  Proteins, 67, 75-83.  
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 code is shown on the right.