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| | <StructureSection load='4p3g' size='340' side='right'caption='[[4p3g]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='4p3g' size='340' side='right'caption='[[4p3g]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p3g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3G FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p3f|4p3f]], [[4p3e|4p3e]]</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=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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0033730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr>
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| - | <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=4p3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3g OCA], [http://pdbe.org/4p3g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3g RCSB], [http://www.ebi.ac.uk/pdbsum/4p3g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] | + | [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] |
| | <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: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grotwinkel, J T]] | + | [[Category: Grotwinkel JT]] |
| - | [[Category: Sinning, I]] | + | [[Category: Sinning I]] |
| - | [[Category: Wild, K]] | + | [[Category: Wild K]] |
| - | [[Category: Chaetomium thermophilum]]
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| - | [[Category: Rna binding protein]]
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| - | [[Category: Srp]]
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| - | [[Category: Srp68]]
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| Structural highlights
Function
G0S5V2_CHATD Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (By similarity).[PIRNR:PIRNR038995]
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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