1OW3

Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP

Summary for 1OW3

• Entry DOI: 10.2210/pdb1ow3/pdb
• Descriptor: Rho-GTPase-activating protein 1, Transforming protein RhoA, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: complex, gtpase, gap, transition state, gene regulation-signaling protein complex, gene regulation/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q07960; Cell membrane; Lipid-anchor; Cytoplasmic side: P61586
• Total number of polymer chains: 2
• Total formula weight: 49759.36

Authors

Graham, D.L.,Lowe, P.N.,Grime, G.W.,Marsh, M.,Rittinger, K.,Smerdon, S.J.,Gamblin, S.J.,Eccleston, J.F. (deposition date: 2003-03-28, release date: 2003-05-06, Last modification date: 2023-08-16)

Primary citation

Graham, D.L.,Lowe, P.N.,Grime, G.W.,Marsh, M.,Rittinger, K.,Smerdon, S.J.,Gamblin, S.J.,Eccleston, J.F.
MgF(3)(-) as a Transition State Analog of Phosphoryl Transfer
Chem.Biol., 9:375-381, 2002

PubMed Abstract: 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 Mg(2+) and F(-) but without Al(3+). The metallofluoride adopts a trigonal planar arrangement instead of the square planar structure of AlF(4)(-). 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.

PubMed: 11927263
DOI: 10.1016/S1074-5521(02)00112-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)