1zo1: Difference between revisions

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[[Image:1zo1.gif|left|200px]]


{{Structure
==IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex==
|PDB= 1zo1 |SIZE=350|CAPTION= <scene name='initialview01'>1zo1</scene>
<SX load='1zo1' size='340' side='right' viewer='molstar' caption='[[1zo1]], [[Resolution|resolution]] 13.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
<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>
|ACTIVITY=
</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>
|GENE=
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo1 OCA], [http://www.ebi.ac.uk/pdbsum/1zo1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zo1 RCSB]</span>
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/1zo1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex'''
==See Also==
 
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
 
__TOC__
==Overview==
</SX>
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==
1ZO1 is a [[Protein complex]] structure of sequences 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].
 
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15935757 15935757]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[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]]
 
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