1zo3

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(New page: 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==
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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.
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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]]
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[[Category: Allen, G.S.]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:39:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:28 2008''

Revision as of 14:17, 21 February 2008


1zo3

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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.

About this Structure

1ZO3 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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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