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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.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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