1n0v
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Crystal structure of elongation factor 2
OverviewOverview
Two crystal structures of yeast translation elongation factor 2 (eEF2) were determined: the apo form at 2.9 A resolution and eEF2 in the presence of the translocation inhibitor sordarin at 2.1 A resolution. 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. The domain rearrangements induced by sordarin binding and the highly ordered drug-binding site observed in the eEF2-sordarin structure provide a high-resolution structural basis for the mechanism of sordarin inhibition. The two structures also emphasize the dynamic nature of the ribosomal translocase.
About this StructureAbout this Structure
1N0V is a Single protein structure of sequence from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 1N0V with [Elongation Factors]. Full crystallographic information is available from OCA.
ReferenceReference
Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase., Jorgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG, Andersen GR, Nat Struct Biol. 2003 May;10(5):379-85. PMID:12692531
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