GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDEGLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE
Structural highlights
1bx9 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
GSTF2_ARATH Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Wagner U, Edwards R, Dixon DP, Mauch F. Probing the diversity of the Arabidopsis glutathione S-transferase gene family. Plant Mol Biol. 2002 Jul;49(5):515-32. PMID:12090627
↑Dixon DP, Sellars JD, Edwards R. The Arabidopsis phi class glutathione transferase AtGSTF2: binding and regulation by biologically active heterocyclic ligands. Biochem J. 2011 Aug 15;438(1):63-70. doi: 10.1042/BJ20101884. PMID:21631432 doi:http://dx.doi.org/10.1042/BJ20101884
