Crystal structure of a mutant elongation factor G trapped with a GTP analogue.
Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome.
Hansson
Sebastian
S
Department of Molecular Biophysics, Lund University, Box 124, S-211 00 Lund, Sweden.
Singh
Ranvir
R
Gudkov
Anatoly T
AT
Liljas
Anders
A
Logan
Derek T
DT
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry; D008969:Molecular Sequence Data; D009154:Mutation; D020653:Peptide Elongation Factor G / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D016963:Thermus thermophilus / Q000201:enzymology*
C503923:GDPNP compound; D020653:Peptide Elongation Factor G; D006160:Guanosine Triphosphate