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| <SX load='3zn8' size='340' side='right' viewer='molstar' caption='[[3zn8]], [[Resolution|resolution]] 12.00Å' scene=''> | | <SX load='3zn8' size='340' side='right' viewer='molstar' caption='[[3zn8]], [[Resolution|resolution]] 12.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3zn8]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/ ], [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895], [https://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus'] and [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZN8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zn8]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus] 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=3ZN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZN8 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 12Å</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Signal-recognition-particle_GTPase Signal-recognition-particle GTPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.4 3.6.5.4] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3zn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn8 OCA], [https://pdbe.org/3zn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zn8 RCSB], [https://www.ebi.ac.uk/pdbsum/3zn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zn8 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=3zn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn8 OCA], [https://pdbe.org/3zn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zn8 RCSB], [https://www.ebi.ac.uk/pdbsum/3zn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zn8 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://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_THEAQ SRP54_THEAQ]] 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).[HAMAP-Rule:MF_00306] [[https://www.uniprot.org/uniprot/FTSY_ECOLI FTSY_ECOLI]] 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). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.<ref>PMID:8194520</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15148364</ref> <ref>PMID:17682051</ref>
| + | [https://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ] 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).[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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| | | |
| ==See Also== | | ==See Also== |
- | *[[Signal recognition particle protein|Signal recognition particle protein]] | + | *[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]] |
- | *[[Signal recognition particle receptor|Signal recognition particle receptor]] | + | *[[Signal recognition particle receptor 3D structures|Signal recognition particle receptor 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
- | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
- | [[Category: Saccharolobus solfataricus]]
| + | |
- | [[Category: Atcc 18824]]
| + | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Signal-recognition-particle GTPase]] | + | [[Category: Saccharolobus solfataricus]] |
- | [[Category: Ariosa, A]] | + | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Berger, I]] | + | [[Category: Ariosa A]] |
- | [[Category: Huard, K]] | + | [[Category: Berger I]] |
- | [[Category: Karuppasamy, M]] | + | [[Category: Huard K]] |
- | [[Category: Knoops, K]] | + | [[Category: Karuppasamy M]] |
- | [[Category: Loeffelholz, O von]]
| + | [[Category: Knoops K]] |
- | [[Category: Schaffitzel, C]] | + | [[Category: Schaffitzel C]] |
- | [[Category: Schoehn, G]] | + | [[Category: Schoehn G]] |
- | [[Category: Shan, S O]] | + | [[Category: Shan SO]] |
- | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
- | [[Category: Hydrolase]] | + | [[Category: Von Loeffelholz O]] |
- | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
SRP54_THEAQ 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).[HAMAP-Rule:MF_00306]
Publication Abstract from PubMed
Signal-recognition particle (SRP)-dependent targeting of translating ribosomes to membranes is a multistep quality-control process. Ribosomes that are translating weakly hydrophobic signal sequences can be rejected from the targeting reaction even after they are bound to the SRP. Here we show that the early complex, formed by Escherichia coli SRP and its receptor FtsY with ribosomes translating the incorrect cargo EspP, is unstable and rearranges inefficiently into subsequent conformational states, such that FtsY dissociation is favored over successful targeting. The N-terminal extension of EspP is responsible for these defects in the early targeting complex. The cryo-electron microscopy structure of this 'false' early complex with EspP revealed an ordered M domain of SRP protein Ffh making two ribosomal contacts, and the NG domains of Ffh and FtsY forming a distorted, flexible heterodimer. Our results provide a structural basis for SRP-mediated signal-sequence selection during recruitment of the SRP receptor.
Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex.,von Loeffelholz O, Knoops K, Ariosa A, Zhang X, Karuppasamy M, Huard K, Schoehn G, Berger I, Shan SO, Schaffitzel C Nat Struct Mol Biol. 2013 Apr 7. doi: 10.1038/nsmb.2546. PMID:23563142[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ von Loeffelholz O, Knoops K, Ariosa A, Zhang X, Karuppasamy M, Huard K, Schoehn G, Berger I, Shan SO, Schaffitzel C. Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex. Nat Struct Mol Biol. 2013 Apr 7. doi: 10.1038/nsmb.2546. PMID:23563142 doi:10.1038/nsmb.2546
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