8f1k

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8f1k]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F1K FirstGlance]. <br>
<table><tr><td colspan='2'>[[8f1k]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F1K FirstGlance]. <br>
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</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>
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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]] 2.8&#8491;</td></tr>
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<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=8f1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f1k OCA], [https://pdbe.org/8f1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f1k RCSB], [https://www.ebi.ac.uk/pdbsum/8f1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f1k ProSAT]</span></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=8f1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f1k OCA], [https://pdbe.org/8f1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f1k RCSB], [https://www.ebi.ac.uk/pdbsum/8f1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f1k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/RPOA_ECOLI RPOA_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059]
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[https://www.uniprot.org/uniprot/RPOZ_ECOLI RPOZ_ECOLI] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.[HAMAP-Rule:MF_00366]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial transcription initiation requires sigma factors for nucleation of the transcription bubble. The canonical housekeeping sigma factor, sigma(70), nucleates DNA melting via recognition of conserved bases of the promoter -10 motif, which are unstacked and captured in pockets of sigma(70). By contrast, the mechanism of transcription bubble nucleation and formation during the unrelated sigma(N)-mediated transcription initiation is poorly understood. Herein, we combine structural and biochemical approaches to establish that sigma(N), like sigma(70), captures a flipped, unstacked base in a pocket formed between its N-terminal region I (RI) and extra-long helix features. Strikingly, RI inserts into the nascent bubble to stabilize the nucleated bubble prior to engagement of the obligate ATPase activator. Our data suggest a general paradigm of transcription initiation that requires sigma factors to nucleate an early melted intermediate prior to productive RNA synthesis.
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A general mechanism for transcription bubble nucleation in bacteria.,Mueller AU, Chen J, Wu M, Chiu C, Nixon BT, Campbell EA, Darst SA Proc Natl Acad Sci U S A. 2023 Apr 4;120(14):e2220874120. doi: , 10.1073/pnas.2220874120. Epub 2023 Mar 27. PMID:36972428<ref>PMID:36972428</ref>
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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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 8f1k" 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

SigN RNA polymerase early-melted intermediate bound to full duplex DNA fragment dhsU36 (-12T)

PDB ID 8f1k

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