4f0b | pdb_00004f0b

Crystal structure of the glutathione transferase URE2P1 from Phanerochaete chrysosporium.

spinqualitylabelsall models 4f0b, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f0b is a 2 chain structure with sequence from Phanerodontia chrysosporium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDS, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I7A570_PHACH Publication Abstract from PubMed 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. Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.,Thuillier A, Roret T, Favier F, Gelhaye E, Jacquot JP, Didierjean C, Morel-Rouhier M FEBS Lett. 2013 Jul 11;587(14):2125-30. doi: 10.1016/j.febslet.2013.05.031. Epub , 2013 May 24. PMID:23711374 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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