4zbb

Crystal structure of the glutathione transferase URE2P8 from Phanerochaete chrysosporium complexed with glutathionyl-S-dinitrobenzene.

spinqualitylabelsall models 4zbb, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zbb is a 4 chain structure with sequence from Phanerodontia chrysosporium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: ACT, CL, GDN, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0R4I985_PHACH Publication Abstract from PubMed 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. Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi.,Roret T, Thuillier A, Favier F, Gelhaye E, Didierjean C, Morel-Rouhier M Fungal Genet Biol. 2015 Oct;83:103-12. doi: 10.1016/j.fgb.2015.09.002. Epub 2015 , Sep 5. PMID:26348000 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA