Crystallization of two glutathione S-transferases from an unusual gene family.
Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64% overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3(1)21 or P3(2)21 (unit-cell parameters a = 49.9, c = 271.8 A at 100 K) and the 1-4 isozyme in P4(1) or P4(3) (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.
Oakley
A J
AJ
Department of Pharmacology/Crystallography Centre, University of Western Australia and the Western Australian Institute for Medical Research, Nedlands WA 6907, Australia.
Jirajaroenrat
K
K
Harnnoi
T
T
Ketterman
A J
AJ
Wilce
M C
MC
D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005982:Glutathione Transferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010575:Pesticides / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D019476:Insect Proteins; D010575:Pesticides; D011994:Recombinant Proteins; D005982:Glutathione Transferase