1zo3: Difference between revisions

Revision as of 06:35, 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:1zo3.png

Template:STRUCTURE 1zo3

The P-site and P/E-site tRNA structures fitted to P/I site codon.The P-site and P/E-site tRNA structures fitted to P/I site codon.

Template:ABSTRACT PUBMED 15935757

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

The cryo-EM structure of a translation initiation complex from Escherichia coli., Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J, Cell. 2005 Jun 3;121(5):703-12. PMID:15935757

Page seeded by OCA on Mon Jul 28 06:35:37 2008

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

OCA

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 {{STRUCTURE_1zo3|  PDB=1zo3  |  SCENE=  }}
-'''The P-site and P/E-site tRNA structures fitted to P/I site codon.'''
+===The P-site and P/E-site tRNA structures fitted to P/I site codon.===
-==Overview==
+<!--
-The 70S ribosome and its complement of factors required for initiation of translation in E. coli were purified separately and reassembled in vitro with GDPNP, producing a stable initiation complex (IC) stalled after 70S assembly. We have obtained a cryo-EM reconstruction of the IC showing IF2*GDPNP at the intersubunit cleft of the 70S ribosome. IF2*GDPNP contacts the 30S and 50S subunits as well as fMet-tRNA(fMet). IF2 here adopts a conformation radically different from that seen in the recent crystal structure of IF2. The C-terminal domain of IF2 binds to the single-stranded portion of fMet-tRNA(fMet), thereby forcing the tRNA into a novel orientation at the P site. The GTP binding domain of IF2 binds to the GTPase-associated center of the 50S subunit in a manner similar to EF-G and EF-Tu. Additionally, we present evidence for the localization of IF1, IF3, one C-terminal domain of L7/L12, and the N-terminal domain of IF2 in the initiation complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_15935757}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15935757 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15935757}}
 ==About this Structure==
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 [[Category: Initiation of protein synthesis]]
 [[Category: Ribosome]]
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