1pn6: Difference between revisions

Revision as of 16:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pn6.png

Template:STRUCTURE 1pn6

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.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.

Template:ABSTRACT PUBMED 12859903

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

Page seeded by OCA on Mon Jul 28 16:22:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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.'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12859903}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12859903 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12859903}}
 ==About this Structure==
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 [[Category: Post-termination complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:16:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:22:17 2008''