View source for 2ob7


==Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM==
<SX load='2ob7' size='340' side='right' viewer='molstar' caption='[[2ob7]], [[Resolution|resolution]] 13.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ob7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OB7 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]] 13.6&#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=2ob7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ob7 OCA], [https://pdbe.org/2ob7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ob7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ob7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ob7 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/SSRP_AQUAE SSRP_AQUAE] Binds specifically to the SsrA RNA (tmRNA) and is required for stable association of SsrA with ribosomes.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ob/2ob7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ob7 ConSurf].
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== Publication Abstract from PubMed ==
A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron microscopy, we obtained a map of the complex composed of a stalled ribosome and small protein B, which appears near the decoding center. This result suggests that, when lacking a codon, the A-site on the small subunit is a target for small protein B. To investigate the role of S1 played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs but in the absence of S1. In this complex, several connections between the 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are no longer found. We propose the unifying concept of scaffolding for the roles of small protein B and S1 in binding of transfer-messenger RNA to the ribosome during trans-translation, and we infer a pathway of sequential binding events in the initial phase of trans-translation.

Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1.,Gillet R, Kaur S, Li W, Hallier M, Felden B, Frank J J Biol Chem. 2007 Mar 2;282(9):6356-63. Epub 2006 Dec 19. PMID:17179154<ref>PMID:17179154</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ob7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Felden B]]
[[Category: Frank J]]
[[Category: Gillet R]]
[[Category: Li W]]