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• W2020086703 abstract "The effect of Mg2+ binding on the conformation of the inactive GDP-bound complex of the heterotrimeric G protein α subunit Giα1 has been investigated by X-ray crystallography. Crystal structures of the Giα1·GDP complex were determined after titration with 5, 10, 100, and 200 mM Mg2+. Comparison of these structures with that of the Mg2+-free complex revealed Mg2+ bound at the same site as observed in the structure of the active, Giα1·GTPγS·Mg2+-bound complex of Giα1, with a similar coordination scheme except for the substitution of a water molecule for an oxygen ligand of the γ-phosphate of Giα1·GTPγS·Mg2+. In contrast to the GDP·Mg2+ complex of Gtα and of other G proteins, switch I residues of Giα1 participate in Mg2+ binding and undergo conformational changes as a consequence of Mg2+ binding. Partial order is induced in switch II, which is disordered in the Mg2+-free complex, but no order is observed in the switch III region. This contrasts with the GDP·Mg2+ complex of Gtα in which both switch II and III switch are ordered. Mg2+ binding also induces binding of an SO42- molecule to the active site in a manner which may mimic a Giα1·GDP·PO42-·Mg2+ product complex. Implications of these findings are discussed." @default.
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• W2020086703 date "1998-09-15" @default.
• W2020086703 modified "2023-10-18" @default.
• W2020086703 title "Crystal Structures of the G Protein G_iα1 Complexed with GDP and Mg²⁺: A Crystallographic Titration Experiment" @default.
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• W2020086703 doi "https://doi.org/10.1021/bi9810306" @default.
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