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| | <StructureSection load='5l3v' size='340' side='right'caption='[[5l3v]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5l3v' size='340' side='right'caption='[[5l3v]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l3v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5L3V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l3v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L3V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">srp54, SSO0971 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=5l3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3v OCA], [http://pdbe.org/5l3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l3v RCSB], [http://www.ebi.ac.uk/pdbsum/5l3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3v 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=5l3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3v OCA], [https://pdbe.org/5l3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l3v RCSB], [https://www.ebi.ac.uk/pdbsum/5l3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SRP54_SULSO SRP54_SULSO]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity). | + | [https://www.uniprot.org/uniprot/SRP54_SACS2 SRP54_SACS2] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.[HAMAP-Rule:MF_00306] |
| | <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: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bange, G]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Sinning, I]] | + | [[Category: Bange G]] |
| - | [[Category: Wild, K]] | + | [[Category: Sinning I]] |
| - | [[Category: Co-translational protein targeting]] | + | [[Category: Wild K]] |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Signal recognition particle]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
SRP54_SACS2 Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.[HAMAP-Rule:MF_00306]
Publication Abstract from PubMed
The signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRalpha in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life. Here, we present the crystal structures of the GTPase heterodimers of archaeal (Sulfolobus solfataricus), eukaryotic (Homo sapiens), and chloroplast (Arabidopsis thaliana) SRP systems. The comprehensive structural comparison combined with Brownian dynamics simulations of TC formation allows for the description of the general blueprint and of specific adaptations of the quasi-symmetric heterodimer. Our work defines conserved external nucleotide-binding sites for SRP GTPase activation by RNA. Structural analyses of the GDP-bound, post-hydrolysis states reveal a conserved, magnesium-sensitive switch within the I-box. Overall, we provide a general model for SRP cycle regulation by RNA.
Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex.,Wild K, Bange G, Motiejunas D, Kribelbauer J, Hendricks A, Segnitz B, Wade RC, Sinning I J Mol Biol. 2016 May 27. pii: S0022-2836(16)30184-X. doi:, 10.1016/j.jmb.2016.05.015. PMID:27241309[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wild K, Bange G, Motiejunas D, Kribelbauer J, Hendricks A, Segnitz B, Wade RC, Sinning I. Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex. J Mol Biol. 2016 May 27. pii: S0022-2836(16)30184-X. doi:, 10.1016/j.jmb.2016.05.015. PMID:27241309 doi:http://dx.doi.org/10.1016/j.jmb.2016.05.015
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