Journal article
Crystallization and preliminary X-ray analysis of glutathione transferases from cyanobacteria
SC Feil, J Tang, G Hansen, MA Gorman, E Wiktelius, G Stenberg, MW Parker
Acta Crystallographica Section F Structural Biology and Crystallization Communications | INT UNION CRYSTALLOGRAPHY | Published : 2009
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 Synechococ..
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Awarded by National Cancer Institute
Awarded by National Institute of General Medical Science
Funding Acknowledgements
This work was supported by the Australian Synchrotron Research Program, which is funded by the Commonwealth of Australia under the Major National Research Facilities Program. Use of the Advanced Photon Source was supported by the US DOE, Basic Energy Sciences, Office of Energy Research. GM/CA CAT has been funded in whole or in part with US Federal funds from the National Cancer Institute (Y1-CO-1020) and the National Institute of General Medical Science (Y1-GM-1104). This work was also supported by a grant from the Australian Research Council. SCF is supported by a National Health and Medical Research Council of Australia (NHMRC) Industry Fellowship. MWP is an Australian Research Council Federation Fellow and an NHMRC Honorary Fellow.