6J3H
Crystal structure of the glutathione S-transferase, CsGST83044, of Ceriporiopsis subvermispora in complex with glutathione
Summary for 6J3H
| Entry DOI | 10.2210/pdb6j3h/pdb |
| Descriptor | Glutathione S-transferase, GLUTATHIONE (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 | 4 |
| Total formula weight | 122787.52 |
| Authors | Osman, W.H.W.,Mikami, B.,Saka, N.,Kondo, K.,Nagata, T.,Katahira, M. (deposition date: 2019-01-04, release date: 2019-05-15, Last modification date: 2023-11-22) |
| Primary citation | Osman, W.H.W.,Mikami, B.,Saka, N.,Kondo, K.,Lin, M.I.,Nagata, T.,Katahira, M. Identification of key residues for activities of atypical glutathione S-transferase of Ceriporiopsis subvermispora, a selective degrader of lignin in woody biomass, by crystallography and functional mutagenesis. Int.J.Biol.Macromol., 132:222-229, 2019 Cited by PubMed Abstract: Ceriporiopsis subvermispora (C. subvermispora) is a selective degrader of lignin in the woody biomass. Glutathione S-transferases (GSTs) are multifunctional enzymes that play important roles in cellular detoxification and metabolism. The crystal structures of a GST of C. subvermispora, CsGST83044, in GSH-free and -bound forms were solved at 1.95 and 2.19 Å resolution, respectively. The structure of the GSH-bound form revealed that CsGST83044 can be categorized as an atypical-type of GST. In the GSH-bound form of CsGST83044, Asn22, Asn24, and Tyr46 are located closest to the sulfur atom and form hydrogen bonds with the thiol group. The functional mutagenesis indicated that they are critical for the enzymatic activities of CsGST83044. The critical residues of an atypical-type GST belonging to the GSTFuA class were revealed for the first time. A previous study indicated that CsGST83044 and another GST, CsGST63524, differ in substrate preference; CsGST83044 prefers smaller substrates than CsGST63524 for its esterase activity. The GSH-bound pocket of CsGST83044 turns out to be small, which may explain the preference for smaller substrates. Protein engineering of GSTs of C. subvermispora in the light of the obtained insight may pave a path in the future for utilization of the woody biomass. PubMed: 30928378DOI: 10.1016/j.ijbiomac.2019.03.199 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
Download full validation report
