Crystallization and preliminary crystallographic analysis of bifunctional gamma-glutamylcysteine synthetase-glutatione synthetase from Streptococcus agalactiae

Yasunori Nakashima; Hiroshi Nii; Blythe E Janowiak; Owen W Griffith; Takao Hibi

doi:10.1107/S1744309109018636

Crystallization and preliminary crystallographic analysis of bifunctional gamma-glutamylcysteine synthetase-glutatione synthetase from Streptococcus agalactiae

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):678-80. doi: 10.1107/S1744309109018636. Epub 2009 Jun 27.

Authors

Yasunori Nakashima¹, Hiroshi Nii, Blythe E Janowiak, Owen W Griffith, Takao Hibi

Affiliation

¹ Department of Bioscience, Fukui Prefectural University, Fukui 910-1195, Japan.

Abstract

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).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray
Glutamate-Cysteine Ligase / chemistry*
Glutathione Synthase / chemistry*
Streptococcus agalactiae / enzymology*

Substances

Glutamate-Cysteine Ligase
Glutathione Synthase