ArticleProtein science : a publication of the Protein Society2001
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 81 citations in OpenAlex.
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- Functional and Structural Diversity of Insect Glutathione S-transferases in Xenobiotic Adaptation.International journal of biological sciences · 2022Review
- Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation ofInternational journal of molecular sciences · 2021Article
- Investigation of the active site of an unclassified glutathione transferase inJournal of pesticide science · 2020Article
- Monomeric Camelus dromedarius GSTM1 at low pH is structurally more thermostable than its native dimeric form.PloS one · 2018Article
- Lactococcus lactis is an Efficient Expression System for Mammalian Membrane Proteins Involved in Liver Detoxification, CYP3A4, and MGST1.Molecular biotechnology · 2016Article
- Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Comparison of topological clustering within protein networks using edge metrics that evaluate full sequence, full structure, and active site microenvironment similarity.Protein science : a publication of the Protein Society · 2015Article
- The still mysterious roles of cysteine-containing glutathione transferases in plants.Frontiers in pharmacology · 2014Review
- The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving force.The Journal of biological chemistry · 2013Article
- Structures of a putative ζ-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Glutathione transferases of Phanerochaete chrysosporium: S-glutathionyl-p-hydroquinone reductase belongs to a new structural class.The Journal of biological chemistry · 2011Article
- Characterization of zebrafish Esrom (Myc-binding protein 2) RCC1-like domain splice variants.Molecular and cellular biochemistry · 2010Article
- Investigating homology between proteins using energetic profiles.PLoS computational biology · 2010Article
- Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.EMBO reports · 2009Article
- The unfoldomics decade: an update on intrinsically disordered proteins.BMC genomics · 2008Article
- A procedure for identifying homologous alternative splicing events.BMC bioinformatics · 2007Article
- Differences in the subunit interface residues of alternatively spliced glutathione transferases affects catalytic and structural functions.The Biochemical journal · 2007Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Glutathione S-transferases (GSTs) are dimeric proteins that play an important role in cellular detoxification. Four GSTs from the mosquito Anopheles dirus species B (Ad), an important malaria vector in South East Asia, are produced by alternate splicing of a single transcription product and were previously shown to have detoxifying activity towards pesticides such as DDT. We have determined the crystal structures for two of these alternatively spliced proteins, AdGST1-3 (complexed with glutathione) and AdGST1-4 (apo form), at 1.75 and 2.45 A resolution, respectively. These GST isozymes show differences from the related GST from the Australian sheep blowfly Lucilia cuprina; in particular, the presence of a C-terminal helix forming part of the active site. This helix causes the active site of the Anopheles GSTs to be enclosed. The glutathione-binding helix alpha2 and flanking residues are disordered in the AdGST1-4 (apo) structure, yet ordered in the AdGST1-3 (GSH-bound) structure, suggesting that insect GSTs operate with an induced fit mechanism similar to that found in the plant phi- and human pi-class GSTs. Despite the high overall sequence identities, the active site residues of AdGST1-4 and AdGST1-3 have different conformations.
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