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| | <StructureSection load='1qzx' size='340' side='right'caption='[[1qzx]], [[Resolution|resolution]] 4.00Å' scene=''> | | <StructureSection load='1qzx' size='340' side='right'caption='[[1qzx]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qzx]] 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=1QZX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QZX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qzx]] 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=1QZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j8m|1j8m]], [[1hq1|1hq1]], [[1qzw|1qzw]]</div></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]] 4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRP54 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=1qzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzx OCA], [https://pdbe.org/1qzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qzx RCSB], [https://www.ebi.ac.uk/pdbsum/1qzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzx ProSAT]</span></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=1qzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzx OCA], [http://pdbe.org/1qzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qzx RCSB], [http://www.ebi.ac.uk/pdbsum/1qzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzx 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] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Montoya, G]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Rosendal, K R]] | + | [[Category: Montoya G]] |
| - | [[Category: Sinning, I]] | + | [[Category: Rosendal KR]] |
| - | [[Category: Wild, K]] | + | [[Category: Sinning I]] |
| - | [[Category: Protein targeting]]
| + | [[Category: Wild K]] |
| - | [[Category: Signal recognition particle]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Srp]]
| + | |
| - | [[Category: Srp54]]
| + | |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Targeting of secretory and membrane proteins by the signal recognition particle (SRP) is evolutionarily conserved, and the multidomain protein SRP54 acts as the key player in SRP-mediated protein transport. Binding of a signal peptide to SRP54 at the ribosome is coordinated with GTP binding and subsequent complex formation with the SRP receptor. Because these functions are localized to distinct domains of SRP54, communication between them is essential. We report the crystal structures of SRP54 from the Archaeon Sulfolobus solfataricus with and without its cognate SRP RNA binding site (helix 8) at 4-A resolution. The two structures show the flexibility of the SRP core and the position of SRP54 relative to the RNA. A long linker helix connects the GTPase (G domain) with the signal peptide binding (M) domain, and a hydrophobic contact between the N and M domains relates the signal peptide binding site to the G domain. Hinge regions are identified in the linker between the G and M domains (292-LGMGD) and in the N-terminal part of the M domain, which allow for structural rearrangements within SRP54 upon signal peptide binding at the ribosome.
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication.,Rosendal KR, Wild K, Montoya G, Sinning I Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14701-6. Epub 2003 Dec 1. PMID:14657338[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rosendal KR, Wild K, Montoya G, Sinning I. Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication. Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14701-6. Epub 2003 Dec 1. PMID:14657338 doi:10.1073/pnas.2436132100
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