View source for 4ue4


==Structural basis for targeting and elongation arrest of Bacillus signal recognition particle==
<SX load='4ue4' size='340' side='right' viewer='molstar' caption='[[4ue4]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7&#8491;</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>
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== Function ==
[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> 
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== 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<ref>PMID:26344568</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
== References ==
<references/>
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Beckert B]]
[[Category: Beckmann R]]
[[Category: Kedrov A]]
[[Category: Kempf G]]
[[Category: Sinning I]]
[[Category: Sohmen D]]
[[Category: Stahlberg H]]
[[Category: Wild K]]
[[Category: Wilson DN]]