The project I work in focuses on the study of the function of conserved residues of human glutathione synthetase (2HGS).  

Glutathione syntethase is an enzyme that catalyzes the glutathione formation from γ–glutamylcysteine and glycine in an ATP-dependent manner.

2HGS has similar core structural elements as the other enzymes from the preATP-grasp superfamily, but the positions of some structural elements have been permuted. The result of the circular permutation causes conformational changes and the best example is the conformational change between Human Glutathione Synthetase and E. Coli Glutathione Synthetase, as shown below.

This movie was created by "The Yale Morph Server (http://molmovdb.org)"

References: 

Polekhina, Board, Gali, Rossjohn, and Parker (1999). The Embo Journal 12(18):3204-13

Echols, Milburn, and Gerstein (2003). Nucleic Acids Res. 31:478-82.

Krebs and Gerstein (2000). Nucleic Acids Res. 28:1665-75. 

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