Crystallization and preliminary crystallographic analysis of bifunctional gamma-glutamylcysteine synthetase-glutatione synthetase from Streptococcus agalactiae.
gamma-Glutamylcysteine synthetase-glutathione synthetase (gammaGCS-GS) is a bifunctional enzyme that catalyzes two consecutive steps of ATP-dependent peptide formation in glutathione biosynthesis. Streptococcus agalactiae gammaGCS-GS is a target for the development of potential therapeutic agents. gammaGCS-GS was crystallized using the sitting-drop vapour-diffusion method. The crystals grew to dimensions of 0.3 x 0.2 x 0.2 mm under reducing conditions with 5 mM TCEP. X-ray data were collected to 2.8 A resolution from a tetragonal crystal that belonged to space group I4(1).
Nakashima
Yasunori
Y
Department of Bioscience, Fukui Prefectural University, Fukui 910-1195, Japan.
Nii
Hiroshi
H
Janowiak
Blythe E
BE
Griffith
Owen W
OW
Hibi
Takao
T
D003460:Crystallization; D018360:Crystallography, X-Ray; D005721:Glutamate-Cysteine Ligase / Q000737:chemistry*; D005981:Glutathione Synthase / Q000737:chemistry*; D013292:Streptococcus agalactiae / Q000201:enzymology*
D005721:Glutamate-Cysteine Ligase; D005981:Glutathione Synthase