Motion in Elongation Factor 2 [ef2]

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Classification [D-h-2]

Structures
1n0u Apo form
1n0v Sordarin-bound

Description
This is the eukaryotic form of ribosomal translocase; the prokaryotic form is EF-G. The sordarin-bound form is hypothesized to be similar to the state of EF2 bound to the ribosome.
Quote from Jorgensen et al. Nature Struct. Bio. 10:379 (2003): "The overall conformation of apo eEF2 is similar to that of its prokaryotic homolog elongation factor G (EF-G) in complex with GDP. Upon sordarin binding, the three tRNA-mimicking C-terminal domains undergo substantial conformational changes, while the three N-terminal domains containing the nucleotide-binding site form an almost rigid unit. The conformation of eEF2 in complex with sordarin is entirely different from known conformations observed in crystal structures of EF-G or from cryo-EM studies of EF-G/70S complexes."

References
Jorgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG, Andersen GR (2003). Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Nat Struct Biol. 10(5):379-85. [Medline info for 12692531]

GO terms associated with structures
Molecular functionGTP binding
Biological processprotein biosynthesis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Elongation Factor 2 1n0v [ C ] 1n0u [ A ] 842



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