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  • Title: Crystallization and preliminary X-ray analysis of glutathione transferases from cyanobacteria.
    Author: Feil SC, Tang J, Hansen G, Gorman MA, Wiktelius E, Stenberg G, Parker MW.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2009 May 01; 65(Pt 5):475-7. PubMed ID: 19407380.
    Abstract:
    Glutathione S-transferases (GSTs) are a group of multifunctional enzymes that are found in animals, plants and microorganisms. Their primary function is to remove toxins derived from exogenous sources or the products of metabolism from the cell. Mammalian GSTs have been extensively studied, in contrast to bacterial GSTs which have received relatively scant attention. A new class of GSTs called Chi has recently been identified in cyanobacteria. Chi GSTs exhibit a high glutathionylation activity towards isothiocyanates, compounds that are normally found in plants. Here, the crystallization of two GSTs are presented: TeGST produced by Thermosynechococcus elongates BP-1 and SeGST from Synechococcus elongates PCC 6301. Both enzymes formed crystals that diffracted to high resolution and appeared to be suitable for further X-ray diffraction studies. The structures of these GSTs may shed further light on the evolution of GST catalytic activity and in particular why these enzymes possess catalytic activity towards plant antimicrobial compounds.
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