4LMV

Crystal structure of glutathione transferase GSTFuA2 from Phanerochaete chrysosporium

Summary for 4LMV

• Entry DOI: 10.2210/pdb4lmv/pdb
• Related: 4F03 4G19
• Descriptor: Glutathione transferase, CITRATE ANION, ACETATE ION (3 entities in total)
• Functional Keywords: gst fold, glutathione transferase, transferase
• Biological source: Phanerochaete chrysosporium
• Total number of polymer chains: 6
• Total formula weight: 172911.24

Authors

Didierjean, C.,Favier, F.,Prosper, P. (deposition date: 2013-07-11, release date: 2014-05-28, Last modification date: 2023-11-08)

Primary citation

Mathieu, Y.,Prosper, P.,Favier, F.,Harvengt, L.,Didierjean, C.,Jacquot, J.P.,Morel-Rouhier, M.,Gelhaye, E.
Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.
Plos One, 8:e80298-e80298, 2013

PubMed Abstract: Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry.

PubMed: 24278272
DOI: 10.1371/journal.pone.0080298

Experimental method

X-RAY DIFFRACTION (3.204 Å)