PDBsum entry 1tcd

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protein Protein-protein interface(s) links
Isomerase PDB id
Protein chains
248 a.a. *
Waters ×165
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Trypanosoma cruzi triosephosphate isomerase
Structure: Triosephosphate isomerase. Chain: a, b. Synonym: tim. Engineered: yes
Source: Trypanosoma cruzi. Organism_taxid: 5693. Strain: mexican ninoa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Homo-Dimer (from PDB file)
1.83Å     R-factor:   0.191     R-free:   0.258
Authors: E.Maldonado,M.Soriano-Garcia,N.Cabrera,G.Garza-Ramos, M.Tuena De Gomez-Puyou,A.Gomez-Puyou,R.Perez-Montfort
Key ref:
E.Maldonado et al. (1998). Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes. J Mol Biol, 283, 193-203. PubMed id: 9761683 DOI: 10.1006/jmbi.1998.2094
29-Jan-98     Release date:   13-Jan-99    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P52270  (TPIS_TRYCR) -  Triosephosphate isomerase, glycosomal
251 a.a.
248 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 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!
  Cellular component     glycosome   2 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  


    Added reference    
DOI no: 10.1006/jmbi.1998.2094 J Mol Biol 283:193-203 (1998)
PubMed id: 9761683  
Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes.
E.Maldonado, M.Soriano-García, A.Moreno, N.Cabrera, G.Garza-Ramos, Gómez-Puyou, A.Gómez-Puyou, R.Perez-Montfort.
The aligned amino acid sequences of TIM from Trypanosoma cruzi (TcTIM) and Trypanosoma brucei (TbTIM) have a positional identity of 68%. The two enzymes have markedly similar catalytic properties. Agents that interact with their interface Cys inhibit TcTIM and TbTIM; and those TIMs that lack this Cys (such as human TIM) are largely or completely insensitive to these agents. The susceptibility of TcTIM to the agents is approximately 100 times higher than that of TbTIM. To ascertain the cause of this large difference, the crystal structure of TcTIM was solved at 1.83 A resolution. The two enzymes are very similar homodimers. In TcTIM and TbTIM their respective Cys, 15 or 14, forms part of the dimer interface. In both, the contacts of the Cys with residues of the other subunit are almost identical. Nevertheless, there are noteworthy differences between the two; the existence of glutamine 18 in TbTIM instead of glutamic acid in TcTIM at the beginning of helix 1 decreases the contacts between this portion of the protein and helix 3 of the other subunit. In addition, TcTIM has proline at position 24 in the first helix of the TIM barrel; this is absent in the other TIM. Pro24 disrupts the regular helix arrangement, making the pitch of this helix 1.2 A longer than in TbTIM. When Pro24 of TcTIM was substituted for Glu, the sensitivity of TcTIM to sulfhydryl reagents increased about fivefold, possibly as a consequence of an increase in the space between the first portion of helix 1 and helix 3 of the other subunit. Therefore, it may be concluded that the geometry of the latter region is central in the accessibility to agents that perturb the interface Cys. In human TIM this region is more compact.
  Selected figure(s)  
Figure 2.
Figure 2. (a) Stereoview of the 3 F[o] -2 F[c]electron density map contoured at 1s of Cys15 of TcTIM and its surrounding loop 3 residues. (b) Stereoview of the interface Cys of TcTIM (orange) and TbTIM (green) and surrounding residues. The oxygen, nitrogen and sulfur atoms are represented in red, blue and yellow, respectively.
Figure 3.
Figure 3. Stereoview of the region between the end of loop 1 in monomer B and a portion of helix 3 of the adjoining subunit. TcTIM and TbTIM are depicted in orange and green, respectively. The color-code for the atoms is as in Figure 2(b).
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1998, 283, 193-203) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21396445 J.Moraes, R.Arreola, N.Cabrera, L.Saramago, D.Freitas, A.Masuda, I.da Silva Vaz, M.Tuena de Gomez-Puyou, R.Perez-Montfort, A.Gomez-Puyou, and C.Logullo (2011).
Structural and biochemical characterization of a recombinant triosephosphate isomerase from Rhipicephalus (Boophilus) microplus.
  Insect Biochem Mol Biol, 41, 400-409.
PDB code: 3th6
20165754 R.Chávez-Calvillo, M.Costas, and J.Hernández-Trujillo (2010).
Theoretical analysis of intermolecular interactions of selected residues of triosephosphate isomerase from Trypanosoma cruzi with its inhibitor 3-(2-benzothiazolylthio)-1-propanesulfonic acid.
  Phys Chem Chem Phys, 12, 2067-2074.  
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.  
17989778 V.Olivares-Illana, A.Rodríguez-Romero, I.Becker, M.Berzunza, J.García, R.Pérez-Montfort, N.Cabrera, F.López-Calahorra, 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, Gómez-Puyou, and A.Gómez-Puyou (2007).
Crosstalk between the subunits of the homodimeric enzyme triosephosphate isomerase.
  Proteins, 67, 75-83.  
12112681 H.Reyes-Vivas, E.Martínez-Martínez, G.Mendoza-Hernández, G.López-Velázquez, R.Pérez-Montfort, M.Tuena de Gómez-Puyou, and A.Gómez-Puyou (2002).
Susceptibility to proteolysis of triosephosphate isomerase from two pathogenic parasites: characterization of an enzyme with an intact and a nicked monomer.
  Proteins, 48, 580-590.  
12006590 K.Maithal, G.Ravindra, H.Balaram, and P.Balaram (2002).
Inhibition of plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine. Electrospray ionization mass spectrometric analysis of differential cysteine reactivities.
  J Biol Chem, 277, 25106-25114.  
11512153 C.L.Verlinde, V.Hannaert, C.Blonski, M.Willson, J.J.Périé, L.A.Fothergill-Gilmore, F.R.Opperdoes, M.H.Gelb, W.G.Hol, and P.A.Michels (2001).
Glycolysis as a target for the design of new anti-trypanosome drugs.
  Drug Resist Updat, 4, 50-65.  
11258928 H.Reyes-Vivas, G.Hernández-Alcantara, G.López-Velazquez, N.Cabrera, R.Pérez-Montfort, Gómez-Puyou, and A.Gómez-Puyou (2001).
Factors that control the reactivity of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi.
  Biochemistry, 40, 3134-3140.  
10591103 D.Maes, J.P.Zeelen, N.Thanki, N.Beaucamp, M.Alvarez, M.H.Thi, J.Backmann, J.A.Martial, L.Wyns, R.Jaenicke, and R.K.Wierenga (1999).
The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
  Proteins, 37, 441-453.
PDB code: 1b9b
10383424 M.Alvarez, J.Wouters, D.Maes, V.Mainfroid, F.Rentier-Delrue, L.Wyns, E.Depiereux, and J.A.Martial (1999).
Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.
  J Biol Chem, 274, 19181-19187.
PDB code: 2btm
10468562 X.G.Gao, E.Maldonado, R.Pérez-Montfort, G.Garza-Ramos, Gómez-Puyou, A.Gómez-Puyou, and A.Rodríguez-Romero (1999).
Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane.
  Proc Natl Acad Sci U S A, 96, 10062-10067.
PDB code: 1ci1
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.