5f0g

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Structure of the glutathione transferase delta 2 from Drosophila melanogasterStructure of the glutathione transferase delta 2 from Drosophila melanogaster

Structural highlights

5f0g is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSTD2_DROME Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028). May be involved in detoxification (PubMed:22082028).[1]

Publication Abstract from PubMed

Glutathione transferases (GSTs) are ubiquitous key enzymes that catalyse the conjugation of glutathione to xenobiotic compounds in the detoxification process. GSTs have been proposed to play a dual role in the signal termination of insect chemodetection by modifying odorant and tasting molecules and by protecting the chemosensory system. Among the 40 GSTs identified in Drosophila melanogaster, the Delta and Epsilon groups are insect-specific. GSTs Delta and Epsilon may have evolved to serve in detoxification, and have been associated with insecticide resistance. Here, we report the heterologous expression and purification of the D. melanogaster GST Delta 2 (GSTD2). We investigated the capacity of GSTD2 to bind tasting molecules. Among them, we found that isothiocyanates (ITC), insecticidal compounds naturally present in cruciferous plant and perceived as bitter, are good substrates for GSTD2. The X-ray structure of GSTD2 was solved, showing the absence of the classical Ser catalytic residue, conserved in the Delta and Epsilon GSTs. Using molecular dynamics, the interaction of ITC with the GSTD2 three-dimensional structure is analysed and discussed. These findings allow us to consider a biological role for GSTD2 in chemoperception, considering GSTD2 expression in the chemosensory organs and the potential consequences of insect exposure to ITC.

Characterization of a Drosophila glutathione transferase involved in isothiocyanate detoxification.,Gonzalez D, Fraichard S, Grassein P, Delarue P, Senet P, Nicolai A, Chavanne E, Mucher E, Artur Y, Ferveur JF, Heydel JM, Briand L, Neiers F Insect Biochem Mol Biol. 2018 Mar 22;95:33-43. doi: 10.1016/j.ibmb.2018.03.004. PMID:29578047[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Saisawang C, Wongsantichon J, Ketterman AJ. A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster. Biochem J. 2012 Feb 15;442(1):181-90. doi: 10.1042/BJ20111747. PMID:22082028 doi:http://dx.doi.org/10.1042/BJ20111747
  2. Gonzalez D, Fraichard S, Grassein P, Delarue P, Senet P, Nicolai A, Chavanne E, Mucher E, Artur Y, Ferveur JF, Heydel JM, Briand L, Neiers F. Characterization of a Drosophila glutathione transferase involved in isothiocyanate detoxification. Insect Biochem Mol Biol. 2018 Mar 22;95:33-43. doi: 10.1016/j.ibmb.2018.03.004. PMID:29578047 doi:http://dx.doi.org/10.1016/j.ibmb.2018.03.004

5f0g, resolution 1.60Å

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