ArticleScientific reports2017
Dead-end complex, lipid interactions and catalytic mechanism of microsomal glutathione transferase 1, an electron crystallography and mutagenesis investigation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- An In Silico Investigation of the Structural and Evolutionary Features of MAPEG Proteins in Bacteria.Current issues in molecular biology · 2026Article
- GSH-Related Enzymes GPx4, Chac1, and GSTs and Redox Regulation of Ferroptosis in Cancer.International journal of molecular sciences · 2026Review
- PEX5 deficiency enhances radiosensitivity via MGST1-GSH detoxifying function and promotes ferroptosis in liver cancer.Science China. Life sciences · 2025Article
- Comprehensive microcrystal electron diffraction sample preparation for cryo-EM.Nature protocols · 2025Review
- Kinetic Behavior of Glutathione Transferases: Understanding Cellular Protection from Reactive Intermediates.Biomolecules · 2024Review
- Cellular Exposure to Chloroacetanilide Herbicides Induces Distinct Protein Destabilization Profiles.ACS chemical biology · 2023Article
- Microsomal glutathione transferase 1 in cancer and the regulation of ferroptosis.Advances in cancer research · 2023Review
- A High-Throughput Search for SFXN1 Physical Partners Led to the Identification of ATAD3, HSD10 and TIM50.Biology · 2022Article
- Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis.Nature communications · 2021Article
- UBXN1 interacts with the S1 protein of transmissible gastroenteritis coronavirus and plays a role in viral replication.Veterinary research · 2019Article
- MGST1, a GSH transferase/peroxidase essential for development and hematopoietic stem cell differentiation.Redox biology · 2018Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microsomal glutathione transferase 1 (MGST1) is a detoxification enzyme belonging to the Membrane Associated Proteins in Eicosanoid and Glutathione Metabolism (MAPEG) superfamily. Here we have used electron crystallography of two-dimensional crystals in order to determine an atomic model of rat MGST1 in a lipid environment. The model comprises 123 of the 155 amino acid residues, two structured phospholipid molecules, two aliphatic chains and one glutathione (GSH) molecule. The functional unit is a homotrimer centered on the crystallographic three-fold axes of the unit cell. The GSH substrate binds in an extended conformation at the interface between two subunits of the trimer supported by new in vitro mutagenesis data. Mutation of Arginine 130 to alanine resulted in complete loss of activity consistent with a role for Arginine 130 in stabilizing the strongly nucleophilic GSH thiolate required for catalysis. Based on the new model and an electron diffraction data set from crystals soaked with trinitrobenzene, that forms a dead-end Meisenheimer complex with GSH, a difference map was calculated. The map reveals side chain movements opening a cavity that defines the second substrate site.
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