6J3E

Crystal structure of an apo form of the glutathione S-transferase, CsGST63524, of Ceriporiopsis subvermispora

Summary for 6J3E

• Entry DOI: 10.2210/pdb6j3e/pdb
• Descriptor: glutathione S-transferase, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: glutathione s-transferase, ceriporiopsis subvermispora, transferase
• Biological source: Ceriporiopsis subvermispora (strain B) (White-rot fungus)
• Total number of polymer chains: 2
• Total formula weight: 58395.94

Authors

Osman, W.H.W.,Mikami, B.,Saka, N.,Kondo, K.,Nagata, T.,Katahira, M. (deposition date: 2019-01-04, release date: 2019-02-27, Last modification date: 2023-11-22)

Primary citation

Osman, W.H.W.,Mikami, B.,Saka, N.,Kondo, K.,Nagata, T.,Katahira, M.
Structure of a serine-type glutathione S-transferase of Ceriporiopsis subvermispora and identification of the enzymatically important non-canonical residues by functional mutagenesis.
Biochem. Biophys. Res. Commun., 510:177-183, 2019

PubMed Abstract: Ceriporiopsis subvermispora (C. subvermispora), one of the white-rot fungi, is known as a selective lignin degrader of the woody biomass. Glutathione S-transferases (GSTs) are multifunctional enzymes that are capable of catalyzing the reactions involved in detoxification and metabolic pathways. In this study, a GST of C. subvermispora, named CsGST63524, was overexpressed in E. coli, and then purified by affinity, anion exchange, and size exclusion column chromatography. The crystal structures of the CsGST63524 in ligand-free and complex with GSH were refined at 2.45 and 2.50 Å resolutions, respectively. The sulfur atom of glutathione forms a hydrogen bond with Ser21 of CsGST63524, indicating it is a serine-type GST. Mutagenesis of Ser21 unexpectedly indicated that this serine residue is not essential for the enzymatic activity of CsGST63524. Comparative sequence and structural analyses, together with functional mutagenesis, newly identified the enzymatically important non-canonical amino acid residues, Asn23 and Tyr45, other than the serine residue.

PubMed: 30683313
DOI: 10.1016/j.bbrc.2019.01.076

Experimental method

X-RAY DIFFRACTION (2.455 Å)