Crystallization and preliminary X-ray analysis of Drosophila glutathione S-transferase-2.
The sigma-class glutathione S-transferase-2 (GST-2) from Drosophila melanogaster is predominantly found within the indirect flight muscles (IFMs), where it is bound to the 'heavy' subunit of the IFM thin filament troponin complex (Tn-H). An N-terminal extension found in GST-2 is unique within the sigma GST class and may be involved in its interaction with Tn-H or modulate its enzymatic function. The recombinant protein has been crystallized at room temperature using ammonium sulfate as precipitant. Synchrotron radiation was used to measure a complete native data set to 1.75 A resolution from flash-cooled crystals. The crystals belong to one of the trigonal space groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 89.7, c = 131.8 A. The self-rotation function is consistent with a GST-2 dimer in the asymmetric unit.
Agianian
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B
Department of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands. b.agianian@chem.uu.nl
Clayton
J D
JD
Leonard
K
K
Tucker
P
P
Bullard
B
B
Gros
P
P
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004331:Drosophila melanogaster / Q000201:enzymology*; D005982:Glutathione Transferase / Q000737:chemistry*; D011487:Protein Conformation
D005982:Glutathione Transferase