PDBsum entry 4zb9

Transferase

PDB id: 4zb9

Contents

Protein chains

219 a.a.

Ligands

GDS ×2

Metals

_CL

Waters ×187

PDB id:

4zb9

Name:

Transferase

Title:

Crystal structure of the glutathione transferase ure2p8 from phanerochaete chrysosporium, with one glutathione disulfide bound per dimer.

Structure:

Pcure2p8. Chain: a, b, c, d. Engineered: yes

Source:

Phanerochaete chrysosporium. Organism_taxid: 5306. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.219 R-free: 0.273

Authors:

T.Roret,C.Didierjean

Key ref:

T.Roret et al. (2015). Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi. Fungal Genet Biol, 83, 103-112. PubMed id: 26348000 DOI: 10.1016/j.fgb.2015.09.002

Date:

14-Apr-15 Release date: 30-Sep-15

Protein chains

A0A0R4I985  (A0A0R4I985_PHACH) -  PcUre2p8 from Phanerodontia chrysosporium

Seq: 223 a.a.

Struc: 219 a.a.

DOI no: 10.1016/j.fgb.2015.09.002

Fungal Genet Biol 83:103-112 (2015)

PubMed id: 26348000

Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi.

T.Roret, A.Thuillier, F.Favier, E.Gelhaye, C.Didierjean, M.Morel-Rouhier.

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.