The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
Elongation factor G (EF-G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF-Tu--whose structure is already known--it is a member of the GTPase superfamily. We have determined the crystal structure of EF-G--GDP from Thermus thermophilus. It is an elongated molecule whose large, N-terminal domain resembles the G domain of EF-Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF-Tu and other G proteins. The tertiary structures of the second domains of EF-G and EF-Tu are nearly identical, but the relative placement of the first two domains in EF-G--GDP resembles that seen in EF-Tu--GTP, not EF-Tu--GDP. The remaining three domains of EF-G look like RNA binding domains, and have no counterparts in EF-Tu.
Czworkowski
J
J
Department of Chemistry, Yale University, New Haven, CT 06520.
Wang
J
J
Steitz
T A
TA
Moore
P B
PB
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010441:Peptide Chain Elongation, Translational; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu / Q000737:chemistry; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D016963:Thermus thermophilus / Q000737:chemistry / Q000201:enzymology*
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D006153:Guanosine Diphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D010444:Peptide Elongation Factor Tu