View source for 8hsh


==Thermus thermophilus RNA polymerase coreenzyme==
<StructureSection load='8hsh' size='340' side='right'caption='[[8hsh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hsh]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HSH FirstGlance]. <br>
</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=8hsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hsh OCA], [https://pdbe.org/8hsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hsh RCSB], [https://www.ebi.ac.uk/pdbsum/8hsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hsh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPOA_THET8 RPOA_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transcription termination is an essential step in transcription by RNA polymerase (RNAP) and crucial for gene regulation. For many bacterial genes, transcription termination is mediated by the adenosine triphosphate-dependent RNA translocase/helicase Rho, which causes RNA/DNA dissociation from the RNAP elongation complex (EC). However, the structural basis of the interplay between Rho and RNAP remains obscure. Here, we report the cryo-electron microscopy structure of the Thermus thermophilus RNAP EC engaged with Rho. The Rho hexamer binds RNAP through the carboxyl-terminal domains, which surround the RNA exit site of RNAP, directing the nascent RNA seamlessly from the RNA exit to its central channel. The beta-flap tip at the RNA exit is critical for the Rho-dependent RNA release, and its deletion causes an alternative Rho-RNAP binding mode, which is irrelevant to termination. The Rho binding site overlaps with the binding sites of other macromolecules, such as ribosomes, providing a general basis of gene regulation.

Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase from Thermus thermophilus.,Murayama Y, Ehara H, Aoki M, Goto M, Yokoyama T, Sekine SI Sci Adv. 2023 Feb 10;9(6):eade7093. doi: 10.1126/sciadv.ade7093. Epub 2023 Feb 8. PMID:36753546<ref>PMID:36753546</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hsh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Ehara H]]
[[Category: Murayama Y]]
[[Category: Sekine S]]