4ZB9
Crystal structure of the glutathione transferase URE2P8 from Phanerochaete chrysosporium, with one glutathione disulfide bound per dimer.
Summary for 4ZB9
| Entry DOI | 10.2210/pdb4zb9/pdb |
| Descriptor | PcUre2p8, OXIDIZED GLUTATHIONE DISULFIDE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | glutathione transferase, gst fold, oxidized glutathione, transferase |
| Biological source | Phanerochaete chrysosporium |
| Total number of polymer chains | 4 |
| Total formula weight | 106080.06 |
| Authors | Roret, T.,Didierjean, C. (deposition date: 2015-04-14, release date: 2015-09-30, Last modification date: 2024-01-10) |
| Primary citation | Roret, T.,Thuillier, A.,Favier, F.,Gelhaye, E.,Didierjean, C.,Morel-Rouhier, M. Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi. Fungal Genet. Biol., 83:103-112, 2015 Cited by PubMed Abstract: The intracellular systems of detoxification are crucial for the survival of wood degrading fungi. Within these systems, glutathione transferases could play a major role since this family of enzymes is specifically extended in lignolytic fungi. In particular the Ure2p class represents one third of the total GST number in Phanerochaete chrysosporium. These proteins have been phylogenetically split into two subclasses called Ure2pA and Ure2pB. Ure2pB can be classified as Nu GSTs because of shared structural and functional features with previously characterized bacterial isoforms. Ure2pA can rather be qualified as Nu-like GSTs since they exhibit a number of differences. Ure2pA possess a classical transferase activity, a more divergent catalytic site and a higher structural flexibility for some of them, compared to Nu GSTs. The characterization of four members of this Ure2pA subclass (PcUre2pA4, PcUre2pA5, PcUre2pA6 and PcUre2pA8) revealed specific functional and structural features, suggesting that these enzymes have rapidly evolved and differentiated, probably to adapt to the complex chemical environment associated with wood decomposition. PubMed: 26348000DOI: 10.1016/j.fgb.2015.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.403 Å) |
Structure validation
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