4p3g

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'''Unreleased structure'''
 
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The entry 4p3g is ON HOLD
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==Structure of the SRP68-RBD from Chaetomium thermophilum==
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<StructureSection load='4p3g' size='340' side='right'caption='[[4p3g]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4p3g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3G FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3g OCA], [https://pdbe.org/4p3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3g RCSB], [https://www.ebi.ac.uk/pdbsum/4p3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G0S5V2_CHATD G0S5V2_CHATD] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (By similarity).[PIRNR:PIRNR038995]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Grotwinkel, J.T., Wild, K., Sinning, I.
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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>
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Description: Structural insights in eukaryotic SRP
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4p3g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
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[[Category: Large Structures]]
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[[Category: Grotwinkel JT]]
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[[Category: Sinning I]]
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[[Category: Wild K]]

Current revision

Structure of the SRP68-RBD from Chaetomium thermophilum

PDB ID 4p3g

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