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| | <StructureSection load='5m72' size='340' side='right'caption='[[5m72]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5m72' size='340' side='right'caption='[[5m72]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m72]] is a 2 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=5M72 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M72 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m72]] is a 2 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=5M72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M72 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRP72 ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m72 OCA], [http://pdbe.org/5m72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m72 RCSB], [http://www.ebi.ac.uk/pdbsum/5m72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m72 ProSAT]</span></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=5m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m72 OCA], [https://pdbe.org/5m72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m72 RCSB], [https://www.ebi.ac.uk/pdbsum/5m72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m72 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN]] Autosomal dominant aplasia and myelodysplasia. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN] Autosomal dominant aplasia and myelodysplasia. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. 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/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. | + | [https://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Signal recognition particle protein|Signal recognition particle protein]] | + | *[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, M M.M]] | + | [[Category: Becker MMM]] |
| - | [[Category: Sinning, I]] | + | [[Category: Sinning I]] |
| - | [[Category: Wild, K]] | + | [[Category: Wild K]] |
| - | [[Category: Protein targeting]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Protein-peptide complex]]
| + | |
| - | [[Category: Signal recognition particle]]
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| - | [[Category: Tetratricopeptide repeat]]
| + | |
| Structural highlights
Disease
SRP72_HUMAN Autosomal dominant aplasia and myelodysplasia. The disease is caused by mutations affecting the gene represented in this entry.
Function
SRP72_HUMAN Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.
Publication Abstract from PubMed
Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K+-turn. In addition, SRP72-RBD remodels the 5f-loop involved in ribosome binding and visualizes SRP RNA plasticity. Docking of the S domain structure into cryo-electron microscopy density maps reveals multiple contact sites between SRP68/72 and the ribosome, and explains the role of SRP72 in the SRP pathway.
Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.,Becker MM, Lapouge K, Segnitz B, Wild K, Sinning I Nucleic Acids Res. 2016 Nov 29. pii: gkw1124. PMID:27899666[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Becker MM, Lapouge K, Segnitz B, Wild K, Sinning I. Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction. Nucleic Acids Res. 2016 Nov 29. pii: gkw1124. PMID:27899666 doi:http://dx.doi.org/10.1093/nar/gkw1124
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