Crystal Structure of Human Class mu Glutathione Transferase GSTM2-2

Raghunathan, Srinivasan; Chandross, Ronald J.; Kretsinger, Robert H.; Allison, Timothy J.; Penington, Christopher J.; Rule, Gordon S.

doi:10.1006/jmbi.1994.1336

Cited by 120 publications

(57 citation statements)

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“…A similar orthorhombic crystal form with four monomers in the asymmetric unit, was previously described for a hGSTM2-2(F214W) glutathione complex. The parameters (a = 56.9, b = 79.7 and c --220.1 A) (Raghunathan et al, 1994) of the mutant complex crystals show significant differences compared to the ligandfree crystals reported here. It is anticipated that conformationally responsive elements in the enzyme will be identified by comparison of the unliganded structure with enzymeinhibitor complexes.…”

Section: Resultscontrasting

confidence: 64%

“…The solution for self-rotation is a single peak with polar angle ~p = 165, ~ = 42, and x = 180 ~:. Attempts are under way to solve the monoclinic crystal structure by molecular replacement using human GSTM2-2(F214W) models available from the previously described orthorhombic crystal form of the complex with glutathione (Raghunathan et aL, 1994).…”

Section: Resultsmentioning

confidence: 99%

“…The structures of unliganded human GSTAI-1 and GST from !j 1998 International Union of Crystallography Printed in Great Britain -all rights reserved Sch&tosoma japonica have been published recently (Cameron et al, 1995;McTigue et al, 1995). For the mu class, only the liganded structures of the rat GST3-3 (currently named the rGSTMI-1) (Ji et al, 1992;: Xiao et al, 1996 and a mutant form of human hGSTM2-2 (F214W) (Raghunathan et al, 1994) have been studied. The crystal structure of the mutant hGSTM2-2 (F214W) complexed with glutathione has been solved in three orthorhombic crystal forms containing a monomer, dimer or tetramer per asymmetric unit to resolutions of 1.85, 3.5 and 2.5,4,, respectively (Raghunathan et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

“…For the mu class, only the liganded structures of the rat GST3-3 (currently named the rGSTMI-1) (Ji et al, 1992;: Xiao et al, 1996 and a mutant form of human hGSTM2-2 (F214W) (Raghunathan et al, 1994) have been studied. The crystal structure of the mutant hGSTM2-2 (F214W) complexed with glutathione has been solved in three orthorhombic crystal forms containing a monomer, dimer or tetramer per asymmetric unit to resolutions of 1.85, 3.5 and 2.5,4,, respectively (Raghunathan et al, 1994). To date, there are no published reports of crystal structures of mu class GST's without GSH or substrate analogues bound, so it remains unclear how substrate binding may affect the conformation of the binding sites of GST's.…”

Section: Introductionmentioning

confidence: 99%

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Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2–2

Patskovska

Fedorov

Patskovsky

et al. 1998

Acta Crystallogr D Biol Cryst

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Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and thc protein isolated from human tissue were indistinguishablc based on physicochemical, enzymatic and immunological criteria. The catalytically active dimeric hGSTM2-2 was crystallized without GSH or other active-site ligands in two crystal forms. Diffraction from form A crystals extends to 2.5 A and is consistent with the °space group P2~ (a =-53.9, b = 81.5, c = 55.6 ,~, /3 = 109.26 A) with two monomers in the asymmetric unit. Diffraction from form B crystals extends to 3 A and is consistent with a space group P21212~ (a = 57.2, b = 80.7, c = 225.9 A) with two dimers in the asymmetric unit. This is the first report of ligand-free mu-class GST crystals, and a comparison with liganded complexes will provide insight into thc structural conscquences of substrate binding which are thought to be important for catalysis.

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Section: Resultscontrasting

confidence: 64%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2–2

Patskovska

Fedorov

Patskovsky

et al. 1998

Acta Crystallogr D Biol Cryst

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“…There are now representative crystal structures for five cytosolic GST classes. These include alphaclass GST'S (Sinning et al, 1993), mu-class GST'S (Ji et al, 1992;Raghunathan et al, 1994;Lira et al, 1994;McTigue et al, 1995), pi-class GST's (Reinemer et al, 1991(Reinemer et al, , 1992Dirr et al, 1994;Garcia-Sfiez et al, 1994), sigma-class GST (Ji et al, 1995) and theta-like GST's (Wilce et al, 1995;Reinemer et al, 1996). The overall polypeptide fold is very similar between the crystal structures but each class exhibits unique features, particularly about the active site and at the C terminus (Wilce & Parker, 1994).…”

Section: Introductionmentioning

confidence: 98%

Preliminary X-ray crystallographic studies of a newly defined human theta-class glutathione transferase

McKinstry

Oakley

Rossjohn

et al. 1998

Acta Crystallogr D Biol Cryst

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Abstract!luman theta-class glutathione S-transferases (GST's) appear to play a critical role in the metabolism of a variety of environmental pollutants but in some cases the products of the reaction are carcinogenic. Crystals of a human theta-class GST, namely hGSTT2-2, have been grown from polyethylene glycol by the hanging-drop vapour-diffusion method. The crystals belong to the trigonal space group P3121 with cell dimensions of a = h = 94.0 and c= 120.5/k. They contain two monomers in the asymmetric unit and diffract to 3.0A resolution.

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Herbicide detoxification by glutathioneS-transferases as implicated from X-ray structures

et al. 1999

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Herbicide selectivity is a major factor in agricultural weed control and results from the differential detoxification ability of plant species. The special agronomic value of plant GSTs originates mainly from their metabolic herbicide detoxification properties that enhance the herbicide tolerance of crops. Glutathione S‐transferases (GSTs) are a ubiquitous family of multifunctional enzymes involved in the metabolization of a broad variety of xenobiotics (eg herbicides in plants) and reactive endogenous compounds through covalent linkage to glutathione. The metabolization of FOE 5043 results in a GSH conjugate that is subsequently degraded by release of the thiadiazole moiety. The comparison of crystal structures of different GST classes, including plant GSTs, provides a model system to understand active‐site interactions on a molecular level. Additional protein structures of three plant GSTs (Arabidopsis thaliana GST, GST I and III from Zea mays var. mutin) in complex with several ligands (S‐hexylglutathione, S‐lactoylglutathione, and FOE 5043) may be tools to supply detailed knowledge for the rational design of new herbicides and GSTs for selectivity optimization in crops. © 1999 Society of Chemical Industry

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Crystal Structure of Human Class mu Glutathione Transferase GSTM2-2

Cited by 120 publications

References 0 publications

Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2–2

Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2–2

Preliminary X-ray crystallographic studies of a newly defined human theta-class glutathione transferase

Herbicide detoxification by glutathioneS-transferases as implicated from X-ray structures

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