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. 2007 Apr 9;7:20. doi: 10.1673/031.007.2001

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© 2007

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Alignments of the deduced amino acid sequences. (A) Homology shared among all three Mayetiola destructor GSTs, MdesGST-1 (AAS00666), MdesGST-2 (DQ662542) and MdesGST-3 (DQ662543). The boxed sequence of MdesGST-2 represents the N-terminal extension constituted by a hydrophobic/acidic motif. (B) Homology of MdesGST-2 with sequences from other insect Sigma GSTs: Musca domestica (P46437), and Drosophila melanogaster (AAM48357). Filled and open circles represent residues that constitute the putative glutathione (GSH) and electrophilic-substrate binding sites, respectively. The putative H-site residue of MdesGST-2 (L62), which also contacts GSH, is indicated by an asterisk. The bulge-inducing residue (G205) of MdesGST-2 is marked with an inverted filled triangle, [continued on next page]