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

Authors :: Nakashima Y
Nii H
Janowiak BE
Griffith OW
Hibi T
Source :: Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2009 Jul 01; Vol. 65 (Pt 7), pp. 678-80. Date of Electronic Publication: 2009 Jun 27.
Publication Year :: 2009
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).

Subjects :: Crystallization
Crystallography, X-Ray
Glutamate-Cysteine Ligase chemistry
Glutathione Synthase chemistry
Streptococcus agalactiae enzymology

Language :: English
ISSN :: 1744-3091
Volume :: 65
Issue :: Pt 7
Database :: MEDLINE
Journal :: Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :: Academic Journal
Accession number :: 19574637
Full Text :: https://doi.org/10.1107/S1744309109018636

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