Motion in Elongation Factor G [efg]

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Classification [D-h-2]


This is the prokaryotic form of ribosomal translocase; the eukaryotic form is EF-2.

A AEvarsson, E Brazhnikov, M Garber, J Zheltonosova, Y Chirgadze, S al-Karadaghi, L A Svensson, A Liljas (1994). Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J, 13:3669-77 [Medline info for 8070397]
M Laurberg, O Kristensen, K Martemyanov, A T Gudkov, I Nagaev, D Hughes, A Liljas (2000). Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. J Mol Biol, 303:593-603 [Medline info for 11054294]
S al-Karadaghi, A Aevarsson, M Garber, J Zheltonosova, A Liljas (1996). The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure, 4:555-65 [Medline info for 8736554]
K A Martemyanov, A S Yarunin, A Liljas, A T Gudkov (1998). An intact conformation at the tip of elongation factor G domain IV is functionally important. FEBS Lett, 434:205-8 [Medline info for 9738479]
J Czworkowski, J Wang, T A Steitz, P B Moore (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. EMBO J, 13:3661-8 [Medline info for 8070396]

GO terms associated with structures
Molecular functionGTP binding, translation elongation factor activity
Biological processprotein biosynthesis, translational elongation


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Best representative
Morph Morph name Structure #1 Structure #2 Residues
EFG 2efg [ A ] 1fnm [ A ] 691

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_