7OPY
Camel GSTM1-1 in complex with S-(p-nitrobenzyl)glutathione
Summary for 7OPY
| Entry DOI | 10.2210/pdb7opy/pdb |
| Descriptor | Glutathione transferase, S-(P-NITROBENZYL)GLUTATHIONE, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | glutathione, detoxification, pesticides, adaptation, transferase |
| Biological source | Camelus dromedarius (Arabian camel) |
| Total number of polymer chains | 4 |
| Total formula weight | 105123.27 |
| Authors | Papageorgiou, A.C.,Poudel, N. (deposition date: 2021-06-02, release date: 2022-02-16, Last modification date: 2024-10-23) |
| Primary citation | Perperopoulou, F.,Poudel, N.,Papageorgiou, A.C.,Ataya, F.S.,Labrou, N.E. Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1. Life, 12:-, 2022 Cited by PubMed Abstract: Glutathione transferases (GSTs; EC. 2.5.1.18) are a large family of multifunctional enzymes that play crucial roles in the metabolism and inactivation of a broad range of xenobiotic compounds. In the present work, we report the kinetic and structural characterization of the isoenzyme GSTM1-1 from (GSTM1-1). The GSΤM1-1 was expressed in BL21 (DE3) and was purified by affinity chromatography. Kinetics analysis showed that the enzyme displays a relative narrow substrate specificity and restricted ability to bind xenobiotic compounds. The crystal structures of GSΤM1-1 were determined by X-ray crystallography in complex with the substrate (GSH) or the reaction product (S-p-nitrobenzyl-GSH), providing snapshots of the induced-fit catalytic mechanism. The thermodynamic stability of GSTM1-1 was investigated using differential scanning fluorimetry (DSF) in the absence and in presence of GSH and S-p-nitrobenzyl-GSH and revealed that the enzyme's structure is significantly stabilized by its ligands. The results of the present study advance the understanding of camelid GST detoxification mechanisms and their contribution to abiotic stress adaptation in harsh desert conditions. PubMed: 35054499DOI: 10.3390/life12010106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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