view article

Figure 2
(a) Overlay of the 2.2 Å resolution apo crystal structure of a putative ζ-class GST from C. immitis in gray with a 1.85 Å resolution glutathione-bound structure in green. Glutathione and sulfate ions are shown in stick representation. An unbiased OMIT map (|Fo| − |Fc|) is shown in green mesh contoured at 2.5σ. (b) Close-up of the overlay shown in (a) showing the large-scale movement of α2 and loops upon glutathione binding. (c) Interactions of glutathione (GSH) with G-site residues. All residues other than Asp122′ are from the same protomer.

ISSN: 2053-230X
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds