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Structures of yeast glutathione‐ S ‐transferase Gtt2 reveal a new catalytic type of GST family
- Source :
- EMBO reports. 10:1320-1326
- Publication Year :
- 2009
- Publisher :
- EMBO, 2009.
-
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.
- Subjects :
- Models, Molecular
Scientific Report
Molecular Sequence Data
Saccharomyces cerevisiae
Crystallography, X-Ray
Biochemistry
Catalysis
Protein Structure, Secondary
Serine
chemistry.chemical_compound
Cytosol
Protein structure
Sequence Analysis, Protein
Genetics
Transferase
Amino Acid Sequence
Site-directed mutagenesis
Molecular Biology
Glutathione Transferase
Alanine
Sequence Homology, Amino Acid
biology
Glutathione
biology.organism_classification
Glutathione S-transferase
chemistry
Multigene Family
biology.protein
Mutant Proteins
Subjects
Details
- ISSN :
- 14693178 and 1469221X
- Volume :
- 10
- Database :
- OpenAIRE
- Journal :
- EMBO reports
- Accession number :
- edsair.doi.dedup.....46cf65f25598509727fd5ef87524153a