1zo1: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1zo1]] is a 3 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1ZO1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1zo1]] is a 3 chain structure with sequence from [https://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 [https://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"><div style='overflow: auto; max-height: 3em;'>[[1z03|1z03]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 13.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo1 OCA], [https://pdbe.org/1zo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1zo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zo1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo1 OCA], [https://pdbe.org/1zo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1zo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zo1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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>  [[https://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]  
[https://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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zo1 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zo1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1zo1" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Allen, G S]]
[[Category: Allen GS]]
[[Category: Ehrenberg, M]]
[[Category: Ehrenberg M]]
[[Category: Frank, J]]
[[Category: Frank J]]
[[Category: Gursky, R]]
[[Category: Gursky R]]
[[Category: Zavialov, A]]
[[Category: Zavialov A]]
[[Category: Cryo-eletron microscopy]]
[[Category: E. coli]]
[[Category: Initiation factor]]
[[Category: Initiation of protein synthesis]]
[[Category: Ribosome]]
[[Category: Translation-rna complex]]

Latest revision as of 09:06, 14 February 2024

IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex

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