Article
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.
Acta crystallographica. Section D, Biological crystallography - 1 Feb 2006
Grahn Elin, Novotny Marian, Jakobsson Emma, Gustafsson Ann, Grehn Leif, Olin Birgit, Madsen Dennis, Wahlberg Mårten, Mannervik Bengt, Kleywegt Gerard J
Abstract excerpt
Human glutathione transferase A1-1 is a well studied enzyme, but despite a wealth of structural and biochemical data a number of aspects of its catalytic function are still poorly understood. Here, five new crystal structures of this enzyme are described that provide several insights. Firstly, the structure of a complex of the wild-type human enzyme with glutathione was determined for the first time at 2.0...
Topics
- Binding Sites
- Crystallography, X-Ray
- Glutathione
- Glutathione Transferase
- Humans
- Isoenzymes
- Models, Molecular
- Mutation
- Protein Structure, Tertiary
- Solvents