Journal article

A structurally derived consensus pattern for theta class glutathione transferases

J Rossjohn, PG Board, MW Parker, MCJ Wilce

PROTEIN ENGINEERING | OXFORD UNIV PRESS UNITED KINGDOM | Published : 1996

Abstract

We have recently determined the first crystal structure of a theta class glutathione transferase. We have aligned the amino acid sequences of members of the family using the crystal structure as a guide. The alignment has revealed a consensus pattern of residues that first identifies a protein as belonging to the glutathione transferase superfamily, and second is able to distinguish theta class members from other classes of glutathione transferases. The consensus residues unique to the theta class are found to cluster mostly on the hydrophilic surface and flanking loops of helix 2, a region found to be structurally diverse amongst crystal structures of the different glutathione transferase c..

View full abstract