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. 1996 Aug 6;93(16):8208–8213. doi: 10.1073/pnas.93.16.8208

Location of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallography.

X Ji 1, E C von Rosenvinge 1, W W Johnson 1, R N Armstrong 1, G L Gilliland 1
PMCID: PMC38648  PMID: 8710848

Abstract

The crystal structure of the sigma class glutathione transferase from squid digestive gland in complex with S-(3-iodobenzyl)glutathione reveals a third binding site for the glutathione conjugate besides the two in the active sites of the dimer. The additional binding site is near the crystallographic two-fold axis between the two alpha 4-turn-alpha 5 motifs. The principal binding interactions with the conjugate include specific electrostatic interactions between the peptide and the two subunits and a hydrophobic cavity found across the two-fold axis that accommodates the 3-iodobenzyl group. Thus, two identical, symmetry-related but mutually exclusive binding modes for the third conjugate are observed. The hydrophobic pocket is about 14 A from the hydroxyl group of Tyr-7 in the active site. This site is a potential transport binding site for hydrophobic molecules or their glutathione conjugates.

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Selected References

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