Crystal Structure of Triosephosphate Isomerase from Trypanosoma cruzi in Hexane

To gain insight into the mechanisms of enzyme catalysis in organic solvents, the x-ray structure of some monomeric enzymes in organic solvents was determined. However, it remained to be explored whether the structure of oligomeric proteins is also amenable to such analysis. The field acquired new pe...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1999-08, Vol.96 (18), p.10062-10067
Main Authors: Gao, Xiu-Gong, Maldonado, Ernesto, Perez-Montfort, Ruy, Garza-Ramos, Georgina, de Gomez-Puyou, Marietta Tuena, Gomez-Puyou, Armando, Rodriguez-Romero, Adela
Format: Article
Language:English
Subjects:
Active sites
Amino Acid Sequence
Animals
Biochemistry
Biological Sciences
Catalytic Domain
Crystal structure
Crystallography, X-Ray
Crystals
Dimerization
Dimers
Enzymes
hexane
Hexanes
Models, Molecular
Molecular Sequence Data
Molecules
Monomers
Protein Conformation
Solvents
Triose-Phosphate Isomerase - chemistry
Trypanosoma cruzi
Trypanosoma cruzi - enzymology
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Summary:To gain insight into the mechanisms of enzyme catalysis in organic solvents, the x-ray structure of some monomeric enzymes in organic solvents was determined. However, it remained to be explored whether the structure of oligomeric proteins is also amenable to such analysis. The field acquired new perspectives when it was proposed that the x-ray structure of enzymes in nonaqueous media could reveal binding sites for organic solvents that in principle could represent the starting point for drug design. Here, a crystal of the dimeric enzyme triosephosphate isomerase from the pathogenic parasite Trypanosoma cruzi was soaked and diffracted in hexane and its structure solved at 2- angstrom resolution. Its overall structure and the dimer interface were not altered by hexane. However, there were differences in the orientation of the side chains of several amino acids, including that of the catalytic Glu-168 in one of the monomers. No hexane molecules were detected in the active site or in the dimer interface. However, three hexane molecules were identified on the surface of the protein at sites, which in the native crystal did not have water molecules. The number of water molecules in the hexane structure was higher than in the native crystal. Two hexanes localized at
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.96.18.10062