1E6B
Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana
Summary for 1E6B
| Entry DOI | 10.2210/pdb1e6b/pdb |
| Descriptor | GLUTATHIONE S-TRANSFERASE, BETA-MERCAPTOETHANOL (3 entities in total) |
| Functional Keywords | transferase |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
| Cellular location | Cytoplasm (By similarity): Q9ZVQ3 |
| Total number of polymer chains | 1 |
| Total formula weight | 24992.66 |
| Authors | Thom, R.,Lapthorn, A.J. (deposition date: 2000-08-10, release date: 2001-06-11, Last modification date: 2025-04-09) |
| Primary citation | Thom, R.,Dixon, D.P.,Edwards, R.,Cole, D.J.,Lapthorn, A.J. The Structure of a Zeta Class Glutathione S-Transferase from Arabidopsis Thaliana: Characterisation of a Gst with Novel Active-Site Architecture and a Putative Role in Tyrosine Catabolism. J.Mol.Biol., 308:949-, 2001 Cited by PubMed Abstract: The cis-trans isomerisation of maleylacetoacetate to fumarylacetoacetate is the penultimate step in the tyrosine/phenylalanine catabolic pathway and has recently been shown to be catalysed by glutathione S-transferase enzymes belonging to the zeta class. Given this primary metabolic role it is unsurprising that zeta class glutathione S-transferases are well conserved over a considerable period of evolution, being found in vertebrates, plants, insects and fungi. The structure of this glutathione S-transferase, cloned from Arabidopsis thaliana, has been solved by single isomorphous replacement with anomalous scattering and refined to a final crystallographic R-factor of 19.6% using data from 25.0 A to 1.65 A. The zeta class enzyme adopts the canonical glutathione S-transferase fold and forms a homodimer with each subunit consisting of 221 residues. In agreement with structures of glutathione S-transferases from the theta and phi classes, a serine residue (Ser17) is present in the active site, at a position that would allow it to stabilise the thiolate anion of glutathione. Site-directed mutagenesis of this residue confirms its importance in catalysis. In addition, the role of a highly conserved cysteine residue (Cys19) present in the active site of the zeta class glutathione S-transferase enzymes is discussed. PubMed: 11352584DOI: 10.1006/JMBI.2001.4638 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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