View source for 1pn6

[[Image:1pn6.gif|left|200px]]

 {{Structure
|PDB= 1pn6 |SIZE=350|CAPTION= <scene name='initialview01'>1pn6</scene>
|SITE= 
|LIGAND= 
|ACTIVITY= 
|GENE= 
}}

'''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.'''


==Overview==
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 Structure==
1PN6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN6 OCA]. 

==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12859903 12859903]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Ehrenberg, M.]]
[[Category: Frank, J.]]
[[Category: Rawat, U.]]
[[Category: Sengupta, J.]]
[[Category: Valle, M.]]
[[Category: Zavialov, A.]]
[[Category: cryo-em]]
[[Category: e coli 70s ribosome]]
[[Category: elongation factor-g]]
[[Category: fitting of crystal structure]]
[[Category: post-termination complex]]

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