4F0B
Crystal structure of the glutathione transferase URE2P1 from Phanerochaete chrysosporium.
Summary for 4F0B
| Entry DOI | 10.2210/pdb4f0b/pdb |
| Related | 4F0C |
| Descriptor | THIOL TRANSFERASE, OXIDIZED GLUTATHIONE DISULFIDE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | thiol transferase, gst fold, oxydized glutathione, transferase |
| Biological source | Phanerochaete chrysosporium |
| Total number of polymer chains | 2 |
| Total formula weight | 52289.45 |
| Authors | Didierjean, C.,Favier, F.,Roret, T. (deposition date: 2012-05-04, release date: 2013-06-12, Last modification date: 2023-09-13) |
| Primary citation | Thuillier, A.,Roret, T.,Favier, F.,Gelhaye, E.,Jacquot, J.P.,Didierjean, C.,Morel-Rouhier, M. Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium. Febs Lett., 587:2125-2130, 2013 Cited by PubMed Abstract: Glutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS-phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi. PubMed: 23711374DOI: 10.1016/j.febslet.2013.05.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report
