The formation of complexes between small G proteins and certain of their effectors can be facilitated by aluminum fluorides. Solution studies suggest that magnesium may be able to replace aluminum in such complexes. We have determined the crystal structure of RhoA.GDP bound to RhoGAP in the presence of Mg2+ and F- but without Al3+. The metallofluoride adopts a trigonal planar arrangement instead of the square planar structure of AlF4-. We have confirmed that these crystals contain magnesium and not aluminum by proton-induced X-ray emission spectroscopy. The structure adopted by GDP.MgF- possesses the stereochemistry and approximate charge expected for the transition state. We suggest that MgF3- may be the reagent of choice for studying phosphoryl transfer reactions.
Graham, D. L., Lowe, P. N., Grime, G. W., Marsh, M., Rittinger, K., Smerdon, S. J., … Eccleston, J. F. (2002). MgF3- as a Transition State Analog of Phosphoryl Transfer. Chemistry and Biology, 9(3), 375–381. https://doi.org/10.1016/S1074-5521(02)00112-6