View source for 4p3e


==Structure of the human SRP S domain==
<StructureSection load='4p3e' size='340' side='right'caption='[[4p3e]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4p3e]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3E 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]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4p3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3e OCA], [https://pdbe.org/4p3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3e RCSB], [https://www.ebi.ac.uk/pdbsum/4p3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SRP19_HUMAN SRP19_HUMAN] Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The signal recognition particle (SRP) is central to membrane protein targeting; SRP RNA is essential for SRP assembly, elongation arrest, and activation of SRP guanosine triphosphatases. In eukaryotes, SRP function relies on the SRP68-SRP72 heterodimer. We present the crystal structures of the RNA-binding domain of SRP68 (SRP68-RBD) alone and in complex with SRP RNA and SRP19. SRP68-RBD is a tetratricopeptide-like module that binds to a RNA three-way junction, bends the RNA, and inserts an alpha-helical arginine-rich motif (ARM) into the major groove. The ARM opens the conserved 5f RNA loop, which in ribosome-bound SRP establishes a contact to ribosomal RNA. Our data provide the structural basis for eukaryote-specific, SRP68-driven RNA remodeling required for protein translocation.

SRP RNA remodeling by SRP68 explains its role in protein translocation.,Grotwinkel JT, Wild K, Segnitz B, Sinning I Science. 2014 Apr 4;344(6179):101-4. doi: 10.1126/science.1249094. PMID:24700861<ref>PMID:24700861</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4p3e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Grotwinkel JT]]
[[Category: Sinning I]]
[[Category: Wild K]]