3ERG

Crystal structure of Gtt2 from Saccharomyces cerevisiae in complex with glutathione sulfnate

Summary for 3ERG

• Entry DOI: 10.2210/pdb3erg/pdb
• Related: 3ERF
• Descriptor: Glutathione S-transferase 2, GLUTATHIONE SULFONIC ACID (3 entities in total)
• Functional Keywords: glutathione s-transferase, gtt2, yeast, transferase
• Biological source: Saccharomyces cerevisiae
• Total number of polymer chains: 2
• Total formula weight: 53463.89

Authors

Ma, X.X.,Jiang, Y.L.,He, Y.X.,Chen, Y.X.,Zhou, C.Z. (deposition date: 2008-10-02, release date: 2009-10-13, Last modification date: 2025-05-07)

Primary citation

Ma, X.X.,Jiang, Y.L.,He, Y.X.,Bao, R.,Chen, Y.X.,Zhou, C.Z.
Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.
Embo Rep., 10:1320-1326, 2009

PubMed Abstract: Glutathione-S-transferases (GSTs) are ubiquitous detoxification enzymes that catalyse the conjugation of electrophilic substrates to glutathione. Here, we present the crystal structures of Gtt2, a GST of Saccharomyces cerevisiae, in apo and two ligand-bound forms, at 2.23 A, 2.20 A and 2.10 A, respectively. Although Gtt2 has the overall structure of a GST, the absence of the classic catalytic essential residues--tyrosine, serine and cysteine--distinguishes it from all other cytosolic GSTs of known structure. Site-directed mutagenesis in combination with activity assays showed that instead of the classic catalytic residues, a water molecule stabilized by Ser129 and His123 acts as the deprotonator of the glutathione sulphur atom. Furthermore, only glycine and alanine are allowed at the amino-terminus of helix-alpha1 because of stereo-hindrance. Taken together, these results show that yeast Gtt2 is a novel atypical type of cytosolic GST.

PubMed: 19851333
DOI: 10.1038/embor.2009.216

Experimental method

X-RAY DIFFRACTION (2.2 Å)