1zo1

<table><tr><td colspan='2'>[[1zo1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZO1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZO1 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z03|1z03]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1zo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo1 OCA], [http://pdbe.org/1zo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1zo1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zo1 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/IF1_ECOLI IF1_ECOLI]] No specific function has so far been attributed to this initiation factor; however, it seems to stimulate more or less all the activities of the other two initiation factors, IF-2 and IF-3.<ref>PMID:376343</ref> [[http://www.uniprot.org/uniprot/IF2_ECOLI IF2_ECOLI]] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.[HAMAP-Rule:MF_00100_B]

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== Publication Abstract from PubMed ==

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 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<ref>PMID:15935757</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Allen, G S]]

[[Category: Ehrenberg, M]]

[[Category: Frank, J]]

[[Category: Gursky, R]]

[[Category: Zavialov, A]]

[[Category: Translation-rna complex]]