1d7q: Difference between revisions

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[[Image:1d7q.jpg|left|200px]]


{{Structure
==HUMAN TRANSLATION INITIATION FACTOR EIF1A==
|PDB= 1d7q |SIZE=350|CAPTION= <scene name='initialview01'>1d7q</scene>
<StructureSection load='1d7q' size='340' side='right'caption='[[1d7q]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1d7q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D7Q FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1d7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7q OCA], [https://pdbe.org/1d7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d7q RCSB], [https://www.ebi.ac.uk/pdbsum/1d7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d7q ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7q OCA], [http://www.ebi.ac.uk/pdbsum/1d7q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d7q RCSB]</span>
[https://www.uniprot.org/uniprot/IF1AX_HUMAN IF1AX_HUMAN] Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
}}
== 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/d7/1d7q_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=1d7q ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The translation initiation factor eIF1A is necessary for directing the 43S preinitiation complex from the 5' end of the mRNA to the initiation codon in a process termed scanning. We have determined the solution structure of human eIF1A, which reveals an oligonucleotide-binding (OB) fold and an additional domain. NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding. The RNA binding surface extends over a large area covering the canonical OB fold binding site as well as a groove leading to the second domain. Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro.


'''HUMAN TRANSLATION INITIATION FACTOR EIF1A'''
The eIF1A solution structure reveals a large RNA-binding surface important for scanning function.,Battiste JL, Pestova TV, Hellen CU, Wagner G Mol Cell. 2000 Jan;5(1):109-19. PMID:10678173<ref>PMID:10678173</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1d7q" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The translation initiation factor eIF1A is necessary for directing the 43S preinitiation complex from the 5' end of the mRNA to the initiation codon in a process termed scanning. We have determined the solution structure of human eIF1A, which reveals an oligonucleotide-binding (OB) fold and an additional domain. NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding. The RNA binding surface extends over a large area covering the canonical OB fold binding site as well as a groove leading to the second domain. Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro.
*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
 
== References ==
==About this Structure==
<references/>
1D7Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7Q OCA].
__TOC__
 
</StructureSection>
==Reference==
The eIF1A solution structure reveals a large RNA-binding surface important for scanning function., Battiste JL, Pestova TV, Hellen CU, Wagner G, Mol Cell. 2000 Jan;5(1):109-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10678173 10678173]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Battiste, J L.]]
[[Category: Battiste JL]]
[[Category: Hellen, C U.T.]]
[[Category: Hellen CUT]]
[[Category: Pestova, T V.]]
[[Category: Pestova TV]]
[[Category: Wagner, G.]]
[[Category: Wagner G]]
[[Category: beta-barrel]]
[[Category: ob-fold]]
[[Category: rna-binding protein]]
 
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