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| | <SX load='4ue4' size='340' side='right' viewer='molstar' caption='[[4ue4]], [[Resolution|resolution]] 7.00Å' scene=''> | | <SX load='4ue4' size='340' side='right' viewer='molstar' caption='[[4ue4]], [[Resolution|resolution]] 7.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ue4]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168] and [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UE4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4UE4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ue4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UE4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ue5|4ue5]]</td></tr> | + | </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=4ue4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ue4 OCA], [https://pdbe.org/4ue4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ue4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ue4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ue4 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=4ue4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ue4 OCA], [http://pdbe.org/4ue4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ue4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ue4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ue4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SRP54_BACSU SRP54_BACSU]] 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. Interaction with FtsY 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 (Probable).<ref>PMID:7511896</ref> | + | [https://www.uniprot.org/uniprot/FTSQ_ECOLI FTSQ_ECOLI] Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.[HAMAP-Rule:MF_00911]<ref>PMID:17185541</ref> <ref>PMID:19233928</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Bacsu]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beckert, B]] | + | [[Category: Beckert B]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Beckmann R]] |
| - | [[Category: Kedrov, A]] | + | [[Category: Kedrov A]] |
| - | [[Category: Kempf, G]] | + | [[Category: Kempf G]] |
| - | [[Category: Sinning, I]] | + | [[Category: Sinning I]] |
| - | [[Category: Sohmen, D]] | + | [[Category: Sohmen D]] |
| - | [[Category: Stahlberg, H]] | + | [[Category: Stahlberg H]] |
| - | [[Category: Wild, K]] | + | [[Category: Wild K]] |
| - | [[Category: Wilson, D N]] | + | [[Category: Wilson DN]] |
| - | [[Category: Mifm stalling]]
| + | |
| - | [[Category: Stalled-ribosome]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translocation]]
| + | |
| Structural highlights
Function
FTSQ_ECOLI Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.[HAMAP-Rule:MF_00911][1] [2]
Publication Abstract from PubMed
The signal recognition particle (SRP) recognizes signal sequences of nascent polypeptides and targets ribosome-nascent chain complexes to membrane translocation sites. In eukaryotes, translating ribosomes are slowed down by the Alu domain of SRP to allow efficient targeting. In prokaryotes, however, little is known about the structure and function of Alu domain-containing SRPs. Here, we report a complete molecular model of SRP from the Gram-positive bacterium Bacillus subtilis, based on cryo-EM. The SRP comprises two subunits, 6S RNA and SRP54 or Ffh, and it facilitates elongation slowdown similarly to its eukaryotic counterpart. However, protein contacts with the small ribosomal subunit observed for the mammalian Alu domain are substituted in bacteria by RNA-RNA interactions of 6S RNA with the alpha-sarcin-ricin loop and helices H43 and H44 of 23S rRNA. Our findings provide a structural basis for cotranslational targeting and RNA-driven elongation arrest in prokaryotes.
Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions.,Beckert B, Kedrov A, Sohmen D, Kempf G, Wild K, Sinning I, Stahlberg H, Wilson DN, Beckmann R Nat Struct Mol Biol. 2015 Sep 7. doi: 10.1038/nsmb.3086. PMID:26344568[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ D'Ulisse V, Fagioli M, Ghelardini P, Paolozzi L. Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology. 2007 Jan;153(Pt 1):124-38. doi: 10.1099/mic.0.2006/000265-0. PMID:17185541 doi:http://dx.doi.org/10.1099/mic.0.2006/000265-0
- ↑ Gonzalez MD, Beckwith J. Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J Bacteriol. 2009 Apr;191(8):2815-25. doi: 10.1128/JB.01597-08. Epub 2009 Feb 20. PMID:19233928 doi:http://dx.doi.org/10.1128/JB.01597-08
- ↑ Beckert B, Kedrov A, Sohmen D, Kempf G, Wild K, Sinning I, Stahlberg H, Wilson DN, Beckmann R. Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions. Nat Struct Mol Biol. 2015 Sep 7. doi: 10.1038/nsmb.3086. PMID:26344568 doi:http://dx.doi.org/10.1038/nsmb.3086
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