1n0v: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1fnm|1FNM]], [[1n0u|1N0U]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n0v OCA], [http://www.ebi.ac.uk/pdbsum/1n0v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n0v RCSB]</span> | |||
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[[Category: g-protein cis-proline]] | [[Category: g-protein cis-proline]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:45 2008'' | ||
Revision as of 22:23, 30 March 2008
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| , resolution 2.85Å | |||||||
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| Related: | 1FNM, 1N0U
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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