1bof: Difference between revisions
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'''GI-ALPHA-1 BOUND TO GDP AND MAGNESIUM''' | '''GI-ALPHA-1 BOUND TO GDP AND MAGNESIUM''' | ||
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[[Category: Coleman, D E.]] | [[Category: Coleman, D E.]] | ||
[[Category: Sprang, S R.]] | [[Category: Sprang, S R.]] | ||
[[Category: | [[Category: G protein]] | ||
[[Category: | [[Category: Gtp-ase]] | ||
[[Category: | [[Category: Signal transduction protein]] | ||
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Revision as of 08:46, 2 May 2008
GI-ALPHA-1 BOUND TO GDP AND MAGNESIUM
Overview
The effect of Mg2+ binding on the conformation of the inactive GDP-bound complex of the heterotrimeric G protein alpha subunit Gi alpha 1 has been investigated by X-ray crystallography. Crystal structures of the Gi alpha 1.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, Gi alpha 1. GTP gamma S.Mg2+-bound complex of Gi alpha 1, with a similar coordination scheme except for the substitution of a water molecule for an oxygen ligand of the gamma-phosphate of Gi alpha 1.GTP gamma S. Mg2+. In contrast to the GDP.Mg2+ complex of Gt alpha and of other G proteins, switch I residues of Gi alpha 1 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 Gt alpha 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 Gi alpha 1.GDP.PO42-.Mg2+ product complex. Implications of these findings are discussed.
About this Structure
1BOF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment., Coleman DE, Sprang SR, Biochemistry. 1998 Oct 13;37(41):14376-85. PMID:9772163 Page seeded by OCA on Fri May 2 11:46:04 2008
