Crystallization of two glutathione S-transferases from an unusual gene family

A. J. Oakley, K. Jirajaroenrat, T. Harnnoi, A. J. Ketterman, M. C.J. Wilce

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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 P3121 or P3221 (unit-cell parameters a = 49.9, c = 271.8 Å at 100 K) and the 1-4 isozyme in P41 or P43 (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.

Original languageEnglish
Pages (from-to)870-872
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Issue number6
Publication statusPublished - Jul 4 2001

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Medicine(all)


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