8fiz

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Current revision (06:43, 19 June 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8fiz]] 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=8FIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FIZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[8fiz]] 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=8FIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FIZ FirstGlance]. <br>
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</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=8fiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fiz OCA], [https://pdbe.org/8fiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fiz RCSB], [https://www.ebi.ac.uk/pdbsum/8fiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fiz ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fiz OCA], [https://pdbe.org/8fiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fiz RCSB], [https://www.ebi.ac.uk/pdbsum/8fiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fiz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RS20_ECOLI RS20_ECOLI] Binds directly to 16S ribosomal RNA.[HAMAP-Rule:MF_00500]
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In prokaryotes, translation can occur on mRNA that is being transcribed in a process called coupling. How the ribosome affects the RNA polymerase (RNAP) during coupling is not well understood. Here, we reconstituted the E. coli coupling system and demonstrated that the ribosome can prevent pausing and termination of RNAP and double the overall transcription rate at the expense of fidelity. Moreover, we monitored single RNAPs coupled to ribosomes and show that coupling increases the pause-free velocity of the polymerase and that a mechanical assisting force is sufficient to explain the majority of the effects of coupling. Also, by cryo-EM, we observed that RNAPs with a terminal mismatch adopt a backtracked conformation, while a coupled ribosome allosterically induces these polymerases toward a catalytically active anti-swiveled state. Finally, we demonstrate that prolonged RNAP pausing is detrimental to cell viability, which could be prevented by polymerase reactivation through a coupled ribosome.
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A trailing ribosome speeds up RNA polymerase at the expense of transcript fidelity via force and allostery.,Wee LM, Tong AB, Florez Ariza AJ, Canari-Chumpitaz C, Grob P, Nogales E, Bustamante CJ Cell. 2023 Mar 16;186(6):1244-1262.e34. doi: 10.1016/j.cell.2023.02.008. PMID:36931247<ref>PMID:36931247</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8fiz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Cryo-EM structure of E. coli 70S Ribosome containing mRNA and tRNA (in the transcription-translation complex)

PDB ID 8fiz

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OCA

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