View source for 5gae


==RNC in complex with a translocating SecYEG==
<SX load='5gae' size='340' side='right' viewer='molstar' caption='[[5gae]], [[Resolution|resolution]] 3.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gae]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GAE 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]] 3.33&#8491;</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5gae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gae OCA], [https://pdbe.org/5gae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gae RCSB], [https://www.ebi.ac.uk/pdbsum/5gae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gae ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342]
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== Publication Abstract from PubMed ==
Co-translational protein targeting to membranes is a universally conserved process. Central steps include cargo recognition by the signal recognition particle and handover to the Sec translocon. Here we present snapshots of key co-translational-targeting complexes solved by cryo-electron microscopy at near-atomic resolution, establishing the molecular contacts between the Escherichia coli translating ribosome, the signal recognition particle and the translocon. Our results reveal the conformational changes that regulate the latching of the signal sequence, the release of the heterodimeric domains of the signal recognition particle and its receptor, and the handover of the signal sequence to the translocon. We also observe that the signal recognition particle and the translocon insert-specific structural elements into the ribosomal tunnel to remodel it, possibly to sense nascent chains. Our work provides structural evidence for a conformational state of the signal recognition particle and its receptor primed for translocon binding to the ribosome-nascent chain complex.

Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.,Jomaa A, Boehringer D, Leibundgut M, Ban N Nat Commun. 2016 Jan 25;7:10471. doi: 10.1038/ncomms10471. PMID:26804923<ref>PMID:26804923</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 5gae" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
== References ==
<references/>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Ban N]]
[[Category: Boehringer D]]
[[Category: Jomaa A]]
[[Category: Leibundgut M]]