7obq
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==SRP-SR at the distal site conformation== |
| - | <StructureSection load='7obq' size='340' side='right'caption='[[7obq]]' scene=''> | + | <StructureSection load='7obq' size='340' side='right'caption='[[7obq]], [[Resolution|resolution]] 3.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7obq]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris], [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OBQ FirstGlance]. <br> |
| - | </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=7obq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7obq OCA], [https://pdbe.org/7obq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7obq RCSB], [https://www.ebi.ac.uk/pdbsum/7obq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7obq ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <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=7obq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7obq OCA], [https://pdbe.org/7obq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7obq RCSB], [https://www.ebi.ac.uk/pdbsum/7obq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7obq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SRP19_CANLF SRP19_CANLF] Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:6413076, PubMed:6938958). Binds directly to 7SL RNA (PubMed:6413076). Mediates binding of SRP54 to the SRP complex (PubMed:6413076).<ref>PMID:6413076</ref> <ref>PMID:6938958</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Co-translational protein targeting to membranes by the signal recognition particle (SRP) is a universally conserved pathway from bacteria to humans. In mammals, SRP and its receptor (SR) have many additional RNA features and protein components compared to the bacterial system, which were recently shown to play regulatory roles. Due to its complexity, the mammalian SRP targeting process is mechanistically not well understood. In particular, it is not clear how SRP recognizes translating ribosomes with exposed signal sequences and how the GTPase activity of SRP and SR is regulated. Here, we present electron cryo-microscopy structures of SRP and SRP.SR in complex with the translating ribosome. The structures reveal the specific molecular interactions between SRP and the emerging signal sequence and the elements that regulate GTPase activity of SRP.SR. Our results suggest the molecular mechanism of how eukaryote-specific elements regulate the early and late stages of SRP-dependent protein targeting. | ||
| + | |||
| + | Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.,Jomaa A, Eitzinger S, Zhu Z, Chandrasekar S, Kobayashi K, Shan SO, Ban N Cell Rep. 2021 Jul 13;36(2):109350. doi: 10.1016/j.celrep.2021.109350. PMID:34260909<ref>PMID:34260909</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7obq" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]] | ||
| + | *[[Signal recognition particle receptor 3D structures|Signal recognition particle receptor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Canis lupus familiaris]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Oryctolagus cuniculus]] |
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Ban N]] | ||
| + | [[Category: Jomaa A]] | ||
Current revision
SRP-SR at the distal site conformation
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