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[[Image:2i91.gif|left|200px]]
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{{STRUCTURE_2i91|  PDB=2i91  |  SCENE=  }}
'''60kDa Ro autoantigen in complex with a fragment of misfolded RNA'''


==60kDa Ro autoantigen in complex with a fragment of misfolded RNA==
<StructureSection load='2i91' size='340' side='right'caption='[[2i91]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2i91]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I91 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2i91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i91 OCA], [https://pdbe.org/2i91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i91 RCSB], [https://www.ebi.ac.uk/pdbsum/2i91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i91 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RO60_XENLA RO60_XENLA] RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. May stabilize these RNAs from degradation.  May play roles in cilia formation and/or maintenance (By similarity).
== 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/i9/2i91_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=2i91 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins.


==Overview==
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen.,Fuchs G, Stein AJ, Fu C, Reinisch KM, Wolin SL Nat Struct Mol Biol. 2006 Nov;13(11):1002-9. Epub 2006 Oct 15. PMID:17041599<ref>PMID:17041599</ref>
The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2I91 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I91 OCA].
</div>
<div class="pdbe-citations 2i91" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen., Fuchs G, Stein AJ, Fu C, Reinisch KM, Wolin SL, Nat Struct Mol Biol. 2006 Nov;13(11):1002-9. Epub 2006 Oct 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17041599 17041599]
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Reinisch, K M.]]
[[Category: Reinisch KM]]
[[Category: Stein, A J.]]
[[Category: Stein AJ]]
[[Category: Heat repeat]]
[[Category: Midas motif]]
[[Category: Rossmann-fold]]
[[Category: Von willebrand factor some]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:12:51 2008''

Latest revision as of 10:07, 30 August 2023

60kDa Ro autoantigen in complex with a fragment of misfolded RNA

2i91, resolution 2.65Å

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