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TitleDead-end complex, lipid interactions and catalytic mechanism of microsomal glutathione transferase 1, an electron crystallography and mutagenesis investigation.
Journal, issue, pagesSci Rep, Vol. 7, Issue 1, Page 7897, Year 2017
Publish dateAug 11, 2017
AuthorsQie Kuang / Pasi Purhonen / Johan Ålander / Richard Svensson / Veronika Hoogland / Jens Winerdal / Linda Spahiu / Astrid Ottosson-Wadlund / Caroline Jegerschöld / Ralf Morgenstern / Hans Hebert /
PubMed AbstractMicrosomal 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 ...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.
External linksSci Rep / PubMed:28801553 / PubMed Central
MethodsEM (electron crystallography)
Resolution3.5 Å
Structure data

8076

5i9k

EMDB-8076, PDB-5i9k:
The structure of microsomal glutathione transferase 1
Method: EM (electron crystallography) / Resolution: 3.5 Å

8084

5ia9

EMDB-8084, PDB-5ia9:
The structure of microsomal glutathione transferase 1 in complex with Meisenheimer complex
Method: EM (electron crystallography) / Resolution: 3.5 Å

Chemicals

ChemComp-GSH:
GLUTATHIONE

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-PLM:
PALMITIC ACID

ChemComp-GTD:
1-(S-GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXA-2,5-DIENE

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / Membrane / Enzyme / Four-helical bundle / Trimer / Meisenheimer complex

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