Structures of a putative ζ-class glutathione S-transferase from the pathogenic fungus Coccidioides immitis

Edwards, T.E.; Bryan, C.M.; Leibly, D.J.; Dieterich, S.H.; Abendroth, J.; Sankaran, B.; Sivam, D.; Staker, B.L.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.

doi:10.1107/S1744309111009493

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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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 (|F_o| − |F_c|) 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.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 67| Part 9| August 2011| Pages 1038-1043

doi:10.1107/S1744309111009493

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