2OMA

Crystallographic analysis of a chemically modified triosephosphate isomerase from Trypanosoma cruzi with dithiobenzylamine (DTBA)

Summary for 2OMA

• Entry DOI: 10.2210/pdb2oma/pdb
• Related: 1TCD
• Descriptor: Triosephosphate isomerase, SULFATE ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: triosephosphate isomerase, trypanosoma cruzi, protein interfaces, dithiobisbenzylamine, isomerase
• Biological source: Trypanosoma cruzi
• Cellular location: Glycosome: P52270
• Total number of polymer chains: 2
• Total formula weight: 56037.94

Authors

Rodriguez-Romero, A.,Gomez-Puyou, A. (deposition date: 2007-01-21, release date: 2007-11-20, Last modification date: 2023-08-30)

Primary citation

Olivares-Illana, V.,Rodriguez-Romero, A.,Becker, I.,Berzunza, M.,Garcia, J.,Perez-Montfort, R.,Cabrera, N.,Lopez-Calahorra, F.,de Gomez-Puyou, M.T.,Gomez-Puyou, A.
Perturbation of the Dimer Interface of Triosephosphate Isomerase and its Effect on Trypanosoma cruzi.
PLoS Negl Trop Dis, 1:e1-e1, 2007

PubMed Abstract: Chagas disease affects around 18 million people in the American continent. Unfortunately, there is no satisfactory treatment for the disease. The drugs currently used are not specific and exert serious toxic effects. Thus, there is an urgent need for drugs that are effective. Looking for molecules to eliminate the parasite, we have targeted a central enzyme of the glycolytic pathway: triosephosphate isomerase (TIM). The homodimeric enzyme is catalytically active only as a dimer. Because there are significant differences in the interface of the enzymes from the parasite and humans, we searched for small molecules that specifically disrupt contact between the two subunits of the enzyme from Trypanosoma cruzi but not those of TIM from Homo sapiens (HTIM), and tested if they kill the parasite.

PubMed: 17989778
DOI: 10.1371/journal.pntd.0000001

Experimental method

X-RAY DIFFRACTION (2.15 Å)