Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane.

ABSTRACT: 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-A resolution. Its overall structure and the dimer interface were not altered by hexane. However, there were differenc

SUBMITTER: Gao XG 

PROVIDER: S-EPMC17842 | biostudies-literature | 1999 Aug

REPOSITORIES: biostudies-literature