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1n0v
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(New page: 200px<br /> <applet load="1n0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0v, resolution 2.85Å" /> '''Crystal structure o...)
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Revision as of 06:57, 18 November 2007
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Crystal structure of elongation factor 2
Overview
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 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.
Reference
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
Page seeded by OCA on Sun Nov 18 09:04:03 2007
