1n0v: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1n0v.gif|left|200px]] | [[Image:1n0v.gif|left|200px]] | ||
'''Crystal structure of elongation factor 2''' | {{Structure | ||
|PDB= 1n0v |SIZE=350|CAPTION= <scene name='initialview01'>1n0v</scene>, resolution 2.85Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of elongation factor 2''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1N0V is a [ | 1N0V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1N0V with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0V OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12692531 12692531] | ||
[[Category: Elongation Factors]] | [[Category: Elongation Factors]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| Line 22: | Line 31: | ||
[[Category: g-protein cis-proline]] | [[Category: g-protein cis-proline]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:50:40 2008'' | ||
Revision as of 13:50, 20 March 2008
| |||||||
| , resolution 2.85Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
Page seeded by OCA on Thu Mar 20 12:50:40 2008