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| | ==Structure of the human SRP S domain== | | ==Structure of the human SRP S domain== |
| - | <StructureSection load='4p3e' size='340' side='right' caption='[[4p3e]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='4p3e' size='340' side='right'caption='[[4p3e]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p3e]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3E FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p3f|4p3f]], [[4p3g|4p3g]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRP19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SRP68 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3e OCA], [http://pdbe.org/4p3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3e RCSB], [http://www.ebi.ac.uk/pdbsum/4p3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SRP68_HUMAN SRP68_HUMAN]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. [[http://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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Grotwinkel, J T]] | + | [[Category: Large Structures]] |
| - | [[Category: Sinning, I]] | + | [[Category: Grotwinkel JT]] |
| - | [[Category: Wild, K]] | + | [[Category: Sinning I]] |
| - | [[Category: Rna binding protein-rna complex]] | + | [[Category: Wild K]] |
| - | [[Category: Srp]]
| + | |
| - | [[Category: Srp rna]]
| + | |
| - | [[Category: Srp19]]
| + | |
| - | [[Category: Srp68]]
| + | |
| Structural highlights
Function
SRP19_HUMAN Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grotwinkel JT, Wild K, Segnitz B, Sinning I. SRP RNA remodeling by SRP68 explains its role in protein translocation. Science. 2014 Apr 4;344(6179):101-4. doi: 10.1126/science.1249094. PMID:24700861 doi:http://dx.doi.org/10.1126/science.1249094
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