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| | <StructureSection load='5l3w' size='340' side='right'caption='[[5l3w]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5l3w' size='340' side='right'caption='[[5l3w]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l3w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5L3W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l3w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L3W 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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsY, ATY89_10730, ATZ20_02285 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909])</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=5l3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3w OCA], [http://pdbe.org/5l3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l3w RCSB], [http://www.ebi.ac.uk/pdbsum/5l3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3w 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=5l3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3w OCA], [https://pdbe.org/5l3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l3w RCSB], [https://www.ebi.ac.uk/pdbsum/5l3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A0U3FSX5_9CREN A0A0U3FSX5_9CREN]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).[HAMAP-Rule:MF_00920] | + | [https://www.uniprot.org/uniprot/FTSY_SULAC FTSY_SULAC] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).[HAMAP-Rule:MF_00920] |
| | <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 33909]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bange, G]] | + | [[Category: Sulfolobus acidocaldarius]] |
| - | [[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]]
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| Structural highlights
Function
FTSY_SULAC Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).[HAMAP-Rule:MF_00920]
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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