1pn6: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1fnm|1FNM]], [[1pn7|1PN7]], [[1pn8|1PN8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn6 OCA], [http://www.ebi.ac.uk/pdbsum/1pn6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pn6 RCSB]</span>
}}
}}


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[[Category: post-termination complex]]
[[Category: post-termination complex]]


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Revision as of 23:01, 30 March 2008

File:1pn6.gif


PDB ID 1pn6

Drag the structure with the mouse to rotate
Related: 1FNM, 1PN7, 1PN8


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.


OverviewOverview

During the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratchet-like rotation of the 30S subunit relative to the 50S subunit in the direction of the mRNA movement. By means of cryo-electron microscopy we observe that this rotation is accompanied by a 20 A movement of the L1 stalk of the 50S subunit, implying that this region is involved in the translocation of deacylated tRNAs from the P to the E site. These ribosomal motions can occur only when the P-site tRNA is deacylated. Prior to peptidyl-transfer to the A-site tRNA or peptide removal, the presence of the charged P-site tRNA locks the ribosome and prohibits both of these motions.

About this StructureAbout this Structure

1PN6 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Locking and unlocking of ribosomal motions., Valle M, Zavialov A, Sengupta J, Rawat U, Ehrenberg M, Frank J, Cell. 2003 Jul 11;114(1):123-34. PMID:12859903

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