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• W1844993037 abstract "Research Article15 August 1994free access The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. J. Czworkowski J. Czworkowski Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author J. Wang J. Wang Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author T.A. Steitz T.A. Steitz Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author P.B. Moore P.B. Moore Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author J. Czworkowski J. Czworkowski Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author J. Wang J. Wang Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author T.A. Steitz T.A. Steitz Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author P.B. Moore P.B. Moore Department of Chemistry, Yale University, New Haven, CT 06520. Search for more papers by this author Author Information J. Czworkowski1, J. Wang1, T.A. Steitz1 and P.B. Moore1 1Department of Chemistry, Yale University, New Haven, CT 06520. The EMBO Journal (1994)13:3661-3668https://doi.org/10.1002/j.1460-2075.1994.tb06675.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 13Issue 161 August 1994In this issue RelatedDetailsLoading ..." @default.
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• W1844993037 title "The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution." @default.
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