1N0V

Crystal structure of elongation factor 2

Summary for 1N0V

• Entry DOI: 10.2210/pdb1n0v/pdb
• Related: 1FNM 1N0U
• Descriptor: Elongation factor 2 (1 entity in total)
• Functional Keywords: g-protein cis-proline, translation
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : P32324
• Total number of polymer chains: 2
• Total formula weight: 186814.25

Authors

Joergensen, R.,Ortiz, P.A.,Carr-Schmid, A.,Nissen, P.,Kinzy, T.G.,Andersen, G.R. (deposition date: 2002-10-15, release date: 2002-11-27, Last modification date: 2024-04-03)

Primary citation

Joergensen, R.,Ortiz, P.A.,Carr-Schmid, A.,Nissen, P.,Kinzy, T.G.,Andersen, G.R.
Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase.
Nat.Struct.Biol., 10:379-385, 2003

PubMed Abstract: 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.

PubMed: 12692531
DOI: 10.1038/nsb923

Experimental method

X-RAY DIFFRACTION (2.85 Å)