Differences in the subunit interface residues of alternatively spliced glutathione transferases affects catalytic and structural functions.

ABSTRACT: GSTs (glutathione transferases) are multifunctional widespread enzymes. Currently there are 13 identified classes within this family. Previously most structural characterization has been reported for mammalian Alpha, Mu and Pi class GSTs. In the present study we characterize two enzymes from the insect-specific Delta class, adGSTD3-3 and adGSTD4-4. These two proteins are alternatively spliced products from the same gene and have very similar tertiary structures. Several major contributions to the dimer interface area can be separated into three regions: conserved electrostatic interactions in region 1, hydrophobic interactions in region 2 and an ionic network in region 3. The four amino acid side chains studied in region 1 interact with each other as a planar rectangle. These interactions

SUBMITTER: Piromjitpong J 

PROVIDER: S-EPMC1770856 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature