6flp

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'''Unreleased structure'''
 
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The entry 6flp is ON HOLD
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==CryoEM structure of E.coli RNA polymerase paused elongation complex without RNA hairpin bound to NusA==
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<SX load='6flp' size='340' side='right' viewer='molstar' caption='[[6flp]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6flp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FLP FirstGlance]. <br>
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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]] 4.1&#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>
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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=6flp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6flp OCA], [https://pdbe.org/6flp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6flp RCSB], [https://www.ebi.ac.uk/pdbsum/6flp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6flp ProSAT]</span></td></tr>
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</table>
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== 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transcriptional pausing by RNA polymerases (RNAPs) is a key mechanism to regulate gene expression in all kingdoms of life and is a prerequisite for transcription termination. The essential bacterial transcription factor NusA stimulates both pausing and termination of transcription, thus playing a central role. Here, we report single-particle electron cryo-microscopy reconstructions of NusA bound to paused E. coli RNAP elongation complexes with and without a pause-enhancing hairpin in the RNA exit channel. The structures reveal four interactions between NusA and RNAP that suggest how NusA stimulates RNA folding, pausing, and termination. An asymmetric translocation intermediate of RNA and DNA converts the active site of the enzyme into an inactive state, providing a structural explanation for the inhibition of catalysis. Comparing RNAP at different stages of pausing provides insights on the dynamic nature of the process and the role of NusA as a regulatory factor.
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Authors:
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Structural Basis for NusA Stabilized Transcriptional Pausing.,Guo X, Myasnikov AG, Chen J, Crucifix C, Papai G, Takacs M, Schultz P, Weixlbaumer A Mol Cell. 2018 Mar 1;69(5):816-827.e4. doi: 10.1016/j.molcel.2018.02.008. PMID:29499136<ref>PMID:29499136</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6flp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Guo X]]
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[[Category: Weixlbaumer A]]

Current revision

CryoEM structure of E.coli RNA polymerase paused elongation complex without RNA hairpin bound to NusA

6flp, resolution 4.10Å

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