1zo3: Difference between revisions

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New page: left|200px<br /><applet load="1zo3" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zo3" /> '''The P-site and P/E-site tRNA structures fitt...
 
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==Overview==
==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 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.


==About this Structure==
==About this Structure==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Allen, G.S.]]
[[Category: Allen, G S.]]
[[Category: Ehrenberg, M.]]
[[Category: Ehrenberg, M.]]
[[Category: Frank, J.]]
[[Category: Frank, J.]]
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[[Category: ribosome]]
[[Category: ribosome]]


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Revision as of 17:17, 21 February 2008

File:1zo3.gif


1zo3

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

OverviewOverview

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.

About this StructureAbout this Structure

1ZO3 is a Protein complex structure of sequences from Escherichia coli. 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

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